xyloglucan Search Results


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  • 91
    Megazyme xyloglucan
    NcLPMO9C EPR spectra. a, EPR spectra of 160 μ m Cu 2+ -loaded Nc LPMO9C in the absence ( upper panel ) or presence ( lower panel ) of the soluble substrates cellohexaose (20 mg/ml) or <t>xyloglucan</t> (15 mg/ml). Spectra were recorded at 77 K, 1 milliwatt of
    Xyloglucan, supplied by Megazyme, used in various techniques. Bioz Stars score: 91/100, based on 294 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore xyloglucan
    NcLPMO9C EPR spectra. a, EPR spectra of 160 μ m Cu 2+ -loaded Nc LPMO9C in the absence ( upper panel ) or presence ( lower panel ) of the soluble substrates cellohexaose (20 mg/ml) or <t>xyloglucan</t> (15 mg/ml). Spectra were recorded at 77 K, 1 milliwatt of
    Xyloglucan, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 98 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Megazyme xyloglucan heptasaccharide
    In vitro recognition of <t>xyloglucan.</t> A. ELISA analysis of Ct CBM3a cipA , Ct CBM3a cipA-M5 and LM15 binding to tamarind xyloglucan. B. Competitive-inhibition ELISAs of LM15 and Ct CBM3a cipA binding to immobilised xyloglucan with xyloglucan (XG), xyloglucan <t>heptasaccharide</t> (XXXG), guar galactomannan (GG) and cellohexaose (Cello) in the soluble phase at 25 μg/ml. Y axis represents the percentage of inhibition achieved by the polysaccharides/haptens. Error bars: SD (n=3)
    Xyloglucan Heptasaccharide, supplied by Megazyme, used in various techniques. Bioz Stars score: 88/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Megazyme xyloglucan oligosaccharides
    27 Al-NMR Profile of AlCl 3 in the Presence of Citrate and <t>Xyloglucan.</t>
    Xyloglucan Oligosaccharides, supplied by Megazyme, used in various techniques. Bioz Stars score: 93/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Megazyme chromogenic substrate azo xyloglucan
    27 Al-NMR Profile of AlCl 3 in the Presence of Citrate and <t>Xyloglucan.</t>
    Chromogenic Substrate Azo Xyloglucan, supplied by Megazyme, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Dainippon Sumitomo xyloglucan
    27 Al-NMR Profile of AlCl 3 in the Presence of Citrate and <t>Xyloglucan.</t>
    Xyloglucan, supplied by Dainippon Sumitomo, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Elicityl xyloglucan
    27 Al-NMR Profile of AlCl 3 in the Presence of Citrate and <t>Xyloglucan.</t>
    Xyloglucan, supplied by Elicityl, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore dp10 xyloglucan s
    27 Al-NMR Profile of AlCl 3 in the Presence of Citrate and <t>Xyloglucan.</t>
    Dp10 Xyloglucan S, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Megazyme tamarind seed xyloglucan
    Expression and activity of XTH . a . Expression of Nicotiana tabacum <t>xyloglucan</t> endotransglycosylase (XTH, Genbank Acc AB017025.1 ) in Vvpgip1 lines 37 and 45 relative to the untransformed control (WT). Standard deviation of the mean relative expression of four technical repeats per plant line is shown with error bars . b . Total XTH activity in tobacco leaves determined by a dot-blot enzyme activity assay. Leaves representing leaf position 3 was used for the assay. A two-tailed Student's t-test showed that p
    Tamarind Seed Xyloglucan, supplied by Megazyme, used in various techniques. Bioz Stars score: 88/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Megazyme b xyloglucan
    (WT) and all xxt mutant plants using selected <t>xyloglucan-directed</t> antibodies. Toluidine blue-stained sections of wild-type and
    B Xyloglucan, supplied by Megazyme, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Seikagaku xyloglucan oligosaccharides
    pH and temperature dependence and kinetic parameters of AtXTH3-mediated transglycosylation reaction. ( a ) pH (left) and temperature (right) dependence of AtXTH3-mediated transglycosylation (donor: amorphous cellulose; acceptor: aminopyridyl cellotetraose, GGGG -AP). ( b ) Michaelis constant ( K M ) and turnover number ( k cat ) for acceptor oligosaccharides (left: GGGG -AP; right: XXXG -AP) with amorphous cellulose as the donor substrate. ( c ) Michaelis constant and turnover number for donor substrates (left: cellulose donor and GGGG -AP acceptor; right: <t>xyloglucan</t> donor and XXXG -AP acceptor). The data are presented as the mean ± s.d. from three independent experiments. Different letters in ( a ) denote significant differences as determined by Tukey’s test ( p
    Xyloglucan Oligosaccharides, supplied by Seikagaku, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Epitope Biotech hypocotyl sections xyloglucan
    pH and temperature dependence and kinetic parameters of AtXTH3-mediated transglycosylation reaction. ( a ) pH (left) and temperature (right) dependence of AtXTH3-mediated transglycosylation (donor: amorphous cellulose; acceptor: aminopyridyl cellotetraose, GGGG -AP). ( b ) Michaelis constant ( K M ) and turnover number ( k cat ) for acceptor oligosaccharides (left: GGGG -AP; right: XXXG -AP) with amorphous cellulose as the donor substrate. ( c ) Michaelis constant and turnover number for donor substrates (left: cellulose donor and GGGG -AP acceptor; right: <t>xyloglucan</t> donor and XXXG -AP acceptor). The data are presented as the mean ± s.d. from three independent experiments. Different letters in ( a ) denote significant differences as determined by Tukey’s test ( p
    Hypocotyl Sections Xyloglucan, supplied by Epitope Biotech, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore xylan 1 xyloglucan detection
    The assessment of the quantitative fluorescence signal of <t>xylan-1/xyloglucan</t> by using the corrected total cell fluorescence method (CTCF) with combination of ANOVA statistics analyses. Yellow bars indicate mock-inoculated and PVY-infected cv. Irys (susceptible) potato plants at 10, 14 and 21 days post-inoculation. Green bars represent mock-inoculated and PVY-inoculated Sárpo Mira (resistant) potato plants at 7, 10 and 14 days post-inoculation. Mean values CTCFC were evaluated at the p
    Xylan 1 Xyloglucan Detection, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Megazyme xyloglucan acceptor
    The assessment of the quantitative fluorescence signal of <t>xylan-1/xyloglucan</t> by using the corrected total cell fluorescence method (CTCF) with combination of ANOVA statistics analyses. Yellow bars indicate mock-inoculated and PVY-infected cv. Irys (susceptible) potato plants at 10, 14 and 21 days post-inoculation. Green bars represent mock-inoculated and PVY-inoculated Sárpo Mira (resistant) potato plants at 7, 10 and 14 days post-inoculation. Mean values CTCFC were evaluated at the p
    Xyloglucan Acceptor, supplied by Megazyme, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Danisco xyloglucan endoglucanase
    The assessment of the quantitative fluorescence signal of <t>xylan-1/xyloglucan</t> by using the corrected total cell fluorescence method (CTCF) with combination of ANOVA statistics analyses. Yellow bars indicate mock-inoculated and PVY-infected cv. Irys (susceptible) potato plants at 10, 14 and 21 days post-inoculation. Green bars represent mock-inoculated and PVY-inoculated Sárpo Mira (resistant) potato plants at 7, 10 and 14 days post-inoculation. Mean values CTCFC were evaluated at the p
    Xyloglucan Endoglucanase, supplied by Danisco, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Novozymes xyloglucan specific endo glucanase
    <t>Xyloglucan</t> fragments, released from seedling cell walls by incubation with a xyloglucan-specific <t>endo</t> <t>-glucanase,</t> were separated on a CarboPac PA200 anion-exchange column. The peak areas of xyloglucan-specific fragments was compared between WT and mutant plants in five independent samples. A glucan size standard was separated under identical conditions, and the degree of Glc-polymerization ( DP ) is indicated in the numbers on the x-axes . The major xyloglucan peaks were assigned by comparison with tamarind xyloglucan standard fragments. Shorter fragments, which are less substituted with xylose, are overrepresented in ugd2,3 , whereas longer fragments are slightly underrepresented in ugd2,3 . Statistically significant data ( p
    Xyloglucan Specific Endo Glucanase, supplied by Novozymes, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Xenobiotics paper immobilised xyloglucan
    Dot-blot screening for XET activity in total extracts from diverse plant organs. (a) XET assays in 96-well format, on paper impregnated with 0.3% <t>xyloglucan</t> + 5 μM XGO–SR; (b) control assays on paper impregnated with XGO–SR alone. Rows A–D and E–H show results with low- and high-salt extracts, respectively, from the plant organs listed on the right. The enzyme solutions (4 μl) were incubated on the papers for 13 h at 22 °C. (c) XET assays on paper impregnated with 0.3% xyloglucan + 5 μM XGO–SR. The enzyme extracts (low-salt buffer) were from parsley (P) or asparagus (A), and either undiluted (row ‘1’) or 2–8-fold diluted (rows ‘/2’ to ‘/8’); 4 μl was applied to the paper and incubated at 22 °C for 0.5, 1, 2, 4, 6 or 12 h, as indicated.
    Paper Immobilised Xyloglucan, supplied by Xenobiotics, used in various techniques. Bioz Stars score: 88/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Novo Nordisk xyloglucan endoglucanase
    Transglucanase Action Products Formed In Vivo in E. fluviatile Tissues. (A) January tissue slices were fed with [ 3 H]XXXGol for 20 h, and its covalent incorporation into 6 M NaOH extractable hemicelluloses <t>(xyloglucan</t> or MLG; XET + MXE product) or alkali-inextractable cellulose (putative CXE product) was quantified (linear reaction range). Putative CXE products were then treated with TFA (2 M, 120°C, 1 h) and remaining insoluble 3 H (TFA residue) was reassayed (“deeply sequestered” cellulose–[ 3 H]XXXGol CXE products). (B) Sequential digestion of the TFA-resistant CXE product by lichenase (3 h), <t>cellulase</t> (3 × 3 h), cellulase + cellobiohydrolase (3 h), and 2× cellulase (24 and 48 h). (C) Thin-layer chromatography fingerprints of the digestion products formed from the TFA residues of in - vivo -generated cellulose–[ 3 H]XXXGol by in-vitro digestion with xyloglucan-inactive cellulase (EST, ESB, and GSB; pooled digests 3–5 from (B) ] and the subsequent synergic action of xyloglucan-inactive cellulase + cellobiohydrolase (EST, ESB, and GSB; digest 6). G n XXXGol, hybrid cello-oligosaccharide–xyloglucan heptasaccharide conjugate (where G n = number of glucose units in the cellulosic tail; n = 1–4). The structural diagram shows the expected sites of attack by “C” xyloglucan-inactive cellulose and, subsequently, “B” cellobiohydrolase. Purple arrows show the positions of markers; non-standard abbreviations: IP-ol, isoprimeveritol; Glc-ol, glucitol. (D and E) Similar experiment as in (A) ; however, MXE and XET action were distinguished by lichenase digestion of alkali-extracted hemicelluloses and expressed as amount of [ 3 H]XXXGol incorporated into the HTG products. XET, MXE, and CXE action were thus separately quantified in Equisetum tissues and P. annua (grass) leaves and stems ( n = 4, ±SD). In (D) , statistically significant differences ( p
    Xyloglucan Endoglucanase, supplied by Novo Nordisk, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Megazyme xyloglucan heptasaccharide xxxg
    Transglucanase Action Products Formed In Vivo in E. fluviatile Tissues. (A) January tissue slices were fed with [ 3 H]XXXGol for 20 h, and its covalent incorporation into 6 M NaOH extractable hemicelluloses <t>(xyloglucan</t> or MLG; XET + MXE product) or alkali-inextractable cellulose (putative CXE product) was quantified (linear reaction range). Putative CXE products were then treated with TFA (2 M, 120°C, 1 h) and remaining insoluble 3 H (TFA residue) was reassayed (“deeply sequestered” cellulose–[ 3 H]XXXGol CXE products). (B) Sequential digestion of the TFA-resistant CXE product by lichenase (3 h), <t>cellulase</t> (3 × 3 h), cellulase + cellobiohydrolase (3 h), and 2× cellulase (24 and 48 h). (C) Thin-layer chromatography fingerprints of the digestion products formed from the TFA residues of in - vivo -generated cellulose–[ 3 H]XXXGol by in-vitro digestion with xyloglucan-inactive cellulase (EST, ESB, and GSB; pooled digests 3–5 from (B) ] and the subsequent synergic action of xyloglucan-inactive cellulase + cellobiohydrolase (EST, ESB, and GSB; digest 6). G n XXXGol, hybrid cello-oligosaccharide–xyloglucan heptasaccharide conjugate (where G n = number of glucose units in the cellulosic tail; n = 1–4). The structural diagram shows the expected sites of attack by “C” xyloglucan-inactive cellulose and, subsequently, “B” cellobiohydrolase. Purple arrows show the positions of markers; non-standard abbreviations: IP-ol, isoprimeveritol; Glc-ol, glucitol. (D and E) Similar experiment as in (A) ; however, MXE and XET action were distinguished by lichenase digestion of alkali-extracted hemicelluloses and expressed as amount of [ 3 H]XXXGol incorporated into the HTG products. XET, MXE, and CXE action were thus separately quantified in Equisetum tissues and P. annua (grass) leaves and stems ( n = 4, ±SD). In (D) , statistically significant differences ( p
    Xyloglucan Heptasaccharide Xxxg, supplied by Megazyme, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Megazyme xllg xyloglucan oligosaccharides
    Transglucanase Action Products Formed In Vivo in E. fluviatile Tissues. (A) January tissue slices were fed with [ 3 H]XXXGol for 20 h, and its covalent incorporation into 6 M NaOH extractable hemicelluloses <t>(xyloglucan</t> or MLG; XET + MXE product) or alkali-inextractable cellulose (putative CXE product) was quantified (linear reaction range). Putative CXE products were then treated with TFA (2 M, 120°C, 1 h) and remaining insoluble 3 H (TFA residue) was reassayed (“deeply sequestered” cellulose–[ 3 H]XXXGol CXE products). (B) Sequential digestion of the TFA-resistant CXE product by lichenase (3 h), <t>cellulase</t> (3 × 3 h), cellulase + cellobiohydrolase (3 h), and 2× cellulase (24 and 48 h). (C) Thin-layer chromatography fingerprints of the digestion products formed from the TFA residues of in - vivo -generated cellulose–[ 3 H]XXXGol by in-vitro digestion with xyloglucan-inactive cellulase (EST, ESB, and GSB; pooled digests 3–5 from (B) ] and the subsequent synergic action of xyloglucan-inactive cellulase + cellobiohydrolase (EST, ESB, and GSB; digest 6). G n XXXGol, hybrid cello-oligosaccharide–xyloglucan heptasaccharide conjugate (where G n = number of glucose units in the cellulosic tail; n = 1–4). The structural diagram shows the expected sites of attack by “C” xyloglucan-inactive cellulose and, subsequently, “B” cellobiohydrolase. Purple arrows show the positions of markers; non-standard abbreviations: IP-ol, isoprimeveritol; Glc-ol, glucitol. (D and E) Similar experiment as in (A) ; however, MXE and XET action were distinguished by lichenase digestion of alkali-extracted hemicelluloses and expressed as amount of [ 3 H]XXXGol incorporated into the HTG products. XET, MXE, and CXE action were thus separately quantified in Equisetum tissues and P. annua (grass) leaves and stems ( n = 4, ±SD). In (D) , statistically significant differences ( p
    Xllg Xyloglucan Oligosaccharides, supplied by Megazyme, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Megazyme amyloid xyloglucan
    Transglucanase Action Products Formed In Vivo in E. fluviatile Tissues. (A) January tissue slices were fed with [ 3 H]XXXGol for 20 h, and its covalent incorporation into 6 M NaOH extractable hemicelluloses <t>(xyloglucan</t> or MLG; XET + MXE product) or alkali-inextractable cellulose (putative CXE product) was quantified (linear reaction range). Putative CXE products were then treated with TFA (2 M, 120°C, 1 h) and remaining insoluble 3 H (TFA residue) was reassayed (“deeply sequestered” cellulose–[ 3 H]XXXGol CXE products). (B) Sequential digestion of the TFA-resistant CXE product by lichenase (3 h), <t>cellulase</t> (3 × 3 h), cellulase + cellobiohydrolase (3 h), and 2× cellulase (24 and 48 h). (C) Thin-layer chromatography fingerprints of the digestion products formed from the TFA residues of in - vivo -generated cellulose–[ 3 H]XXXGol by in-vitro digestion with xyloglucan-inactive cellulase (EST, ESB, and GSB; pooled digests 3–5 from (B) ] and the subsequent synergic action of xyloglucan-inactive cellulase + cellobiohydrolase (EST, ESB, and GSB; digest 6). G n XXXGol, hybrid cello-oligosaccharide–xyloglucan heptasaccharide conjugate (where G n = number of glucose units in the cellulosic tail; n = 1–4). The structural diagram shows the expected sites of attack by “C” xyloglucan-inactive cellulose and, subsequently, “B” cellobiohydrolase. Purple arrows show the positions of markers; non-standard abbreviations: IP-ol, isoprimeveritol; Glc-ol, glucitol. (D and E) Similar experiment as in (A) ; however, MXE and XET action were distinguished by lichenase digestion of alkali-extracted hemicelluloses and expressed as amount of [ 3 H]XXXGol incorporated into the HTG products. XET, MXE, and CXE action were thus separately quantified in Equisetum tissues and P. annua (grass) leaves and stems ( n = 4, ±SD). In (D) , statistically significant differences ( p
    Amyloid Xyloglucan, supplied by Megazyme, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore tamarind tamarindus indica xyloglucan
    Transglucanase Action Products Formed In Vivo in E. fluviatile Tissues. (A) January tissue slices were fed with [ 3 H]XXXGol for 20 h, and its covalent incorporation into 6 M NaOH extractable hemicelluloses <t>(xyloglucan</t> or MLG; XET + MXE product) or alkali-inextractable cellulose (putative CXE product) was quantified (linear reaction range). Putative CXE products were then treated with TFA (2 M, 120°C, 1 h) and remaining insoluble 3 H (TFA residue) was reassayed (“deeply sequestered” cellulose–[ 3 H]XXXGol CXE products). (B) Sequential digestion of the TFA-resistant CXE product by lichenase (3 h), <t>cellulase</t> (3 × 3 h), cellulase + cellobiohydrolase (3 h), and 2× cellulase (24 and 48 h). (C) Thin-layer chromatography fingerprints of the digestion products formed from the TFA residues of in - vivo -generated cellulose–[ 3 H]XXXGol by in-vitro digestion with xyloglucan-inactive cellulase (EST, ESB, and GSB; pooled digests 3–5 from (B) ] and the subsequent synergic action of xyloglucan-inactive cellulase + cellobiohydrolase (EST, ESB, and GSB; digest 6). G n XXXGol, hybrid cello-oligosaccharide–xyloglucan heptasaccharide conjugate (where G n = number of glucose units in the cellulosic tail; n = 1–4). The structural diagram shows the expected sites of attack by “C” xyloglucan-inactive cellulose and, subsequently, “B” cellobiohydrolase. Purple arrows show the positions of markers; non-standard abbreviations: IP-ol, isoprimeveritol; Glc-ol, glucitol. (D and E) Similar experiment as in (A) ; however, MXE and XET action were distinguished by lichenase digestion of alkali-extracted hemicelluloses and expressed as amount of [ 3 H]XXXGol incorporated into the HTG products. XET, MXE, and CXE action were thus separately quantified in Equisetum tissues and P. annua (grass) leaves and stems ( n = 4, ±SD). In (D) , statistically significant differences ( p
    Tamarind Tamarindus Indica Xyloglucan, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    NcLPMO9C EPR spectra. a, EPR spectra of 160 μ m Cu 2+ -loaded Nc LPMO9C in the absence ( upper panel ) or presence ( lower panel ) of the soluble substrates cellohexaose (20 mg/ml) or xyloglucan (15 mg/ml). Spectra were recorded at 77 K, 1 milliwatt of

    Journal: The Journal of Biological Chemistry

    Article Title: Structural and Functional Characterization of a Lytic Polysaccharide Monooxygenase with Broad Substrate Specificity *

    doi: 10.1074/jbc.M115.660183

    Figure Lengend Snippet: NcLPMO9C EPR spectra. a, EPR spectra of 160 μ m Cu 2+ -loaded Nc LPMO9C in the absence ( upper panel ) or presence ( lower panel ) of the soluble substrates cellohexaose (20 mg/ml) or xyloglucan (15 mg/ml). Spectra were recorded at 77 K, 1 milliwatt of

    Article Snippet: EPR samples containing 225 μ m apo Nc LPMO9C, 160 μ m Cu2+ -loaded Nc LPMO9C, 160 μ m Cu2+ -loaded Nc LPMO9C and 20 mg/ml cellohexaose (Megazyme International, Ireland), or 160 μ m Cu2+ -loaded Nc LPMO9C and 15 mg/ml xyloglucan isolated from tamarind seeds (Megazyme International) were frozen and stored in liquid nitrogen.

    Techniques: Electron Paramagnetic Resonance

    Comparison of substrate degradation rates. Degradation of 5 mg/ml PASC ( left ) or tamarind xyloglucan ( right ) by 4 μ m Nc LPMO9C with or without (− N ) the CBM domain at 50 °C was monitored by measuring the formation of reducing ends.

    Journal: The Journal of Biological Chemistry

    Article Title: Structural and Functional Characterization of a Lytic Polysaccharide Monooxygenase with Broad Substrate Specificity *

    doi: 10.1074/jbc.M115.660183

    Figure Lengend Snippet: Comparison of substrate degradation rates. Degradation of 5 mg/ml PASC ( left ) or tamarind xyloglucan ( right ) by 4 μ m Nc LPMO9C with or without (− N ) the CBM domain at 50 °C was monitored by measuring the formation of reducing ends.

    Article Snippet: EPR samples containing 225 μ m apo Nc LPMO9C, 160 μ m Cu2+ -loaded Nc LPMO9C, 160 μ m Cu2+ -loaded Nc LPMO9C and 20 mg/ml cellohexaose (Megazyme International, Ireland), or 160 μ m Cu2+ -loaded Nc LPMO9C and 15 mg/ml xyloglucan isolated from tamarind seeds (Megazyme International) were frozen and stored in liquid nitrogen.

    Techniques:

    Thermograms. a, upper panels , binding isotherms with theoretical fits ( lower panels ) obtained for the titration of Nc LPMO9C ( left ) and Nc LPMO9C-N ( right ) into 0.9 μ m xyloglucan ( top ) and 0.146 mg/ml PASC ( bottom ). The concentration of PASC was

    Journal: The Journal of Biological Chemistry

    Article Title: Structural and Functional Characterization of a Lytic Polysaccharide Monooxygenase with Broad Substrate Specificity *

    doi: 10.1074/jbc.M115.660183

    Figure Lengend Snippet: Thermograms. a, upper panels , binding isotherms with theoretical fits ( lower panels ) obtained for the titration of Nc LPMO9C ( left ) and Nc LPMO9C-N ( right ) into 0.9 μ m xyloglucan ( top ) and 0.146 mg/ml PASC ( bottom ). The concentration of PASC was

    Article Snippet: EPR samples containing 225 μ m apo Nc LPMO9C, 160 μ m Cu2+ -loaded Nc LPMO9C, 160 μ m Cu2+ -loaded Nc LPMO9C and 20 mg/ml cellohexaose (Megazyme International, Ireland), or 160 μ m Cu2+ -loaded Nc LPMO9C and 15 mg/ml xyloglucan isolated from tamarind seeds (Megazyme International) were frozen and stored in liquid nitrogen.

    Techniques: Binding Assay, Titration, Concentration Assay

    The effects of CBM and GH incubation on polysaccharides probe binding. A , heat map showing the results of incubating three polysaccharide substrates (arabinoxylan, hydroxyethylcellulose ( HEC ), and xyloglucan) at 0.1 mg/ml with a GH and/or a CBM with specificity

    Journal: The Journal of Biological Chemistry

    Article Title: A New Versatile Microarray-based Method for High Throughput Screening of Carbohydrate-active Enzymes *

    doi: 10.1074/jbc.M114.630673

    Figure Lengend Snippet: The effects of CBM and GH incubation on polysaccharides probe binding. A , heat map showing the results of incubating three polysaccharide substrates (arabinoxylan, hydroxyethylcellulose ( HEC ), and xyloglucan) at 0.1 mg/ml with a GH and/or a CBM with specificity

    Article Snippet: The following defined polysaccharides were used in this work: arabinan (sugar beet), arabinoxylan (wheat flour), β-glucan (barley), β-glucan lichenan (icelandic moss), galactomannan (carob), glucomannan (konjac), pachyman (1,3-β- d -glucan), pectic galactan (lupin), and xyloglucan (tamarind) from Megazyme; gum arabic (acacia tree), hydroxyethylcellulose, and xylan (beechwood) from Sigma-Aldrich; pectin with degrees of methyl esterification (DEs) of 11, 16, and 81% (lime) from DuPont Nutrition Biosciences (Brabrand, Denmark); and feruloylated arabinoxylan (wheat flour) from Institut National de la Recherche Agronomique (Nantes, France).

    Techniques: Incubation, Binding Assay

    Generation of -fold change heat maps from raw data. A–C , representative examples of arrays produced from a series of reactions involving the incubation (5 h at 30 °C) of several substrates at 0.1 mg/ml including xyloglucan, pectin (DE

    Journal: The Journal of Biological Chemistry

    Article Title: A New Versatile Microarray-based Method for High Throughput Screening of Carbohydrate-active Enzymes *

    doi: 10.1074/jbc.M114.630673

    Figure Lengend Snippet: Generation of -fold change heat maps from raw data. A–C , representative examples of arrays produced from a series of reactions involving the incubation (5 h at 30 °C) of several substrates at 0.1 mg/ml including xyloglucan, pectin (DE

    Article Snippet: The following defined polysaccharides were used in this work: arabinan (sugar beet), arabinoxylan (wheat flour), β-glucan (barley), β-glucan lichenan (icelandic moss), galactomannan (carob), glucomannan (konjac), pachyman (1,3-β- d -glucan), pectic galactan (lupin), and xyloglucan (tamarind) from Megazyme; gum arabic (acacia tree), hydroxyethylcellulose, and xylan (beechwood) from Sigma-Aldrich; pectin with degrees of methyl esterification (DEs) of 11, 16, and 81% (lime) from DuPont Nutrition Biosciences (Brabrand, Denmark); and feruloylated arabinoxylan (wheat flour) from Institut National de la Recherche Agronomique (Nantes, France).

    Techniques: Produced, Incubation

    In vitro recognition of xyloglucan. A. ELISA analysis of Ct CBM3a cipA , Ct CBM3a cipA-M5 and LM15 binding to tamarind xyloglucan. B. Competitive-inhibition ELISAs of LM15 and Ct CBM3a cipA binding to immobilised xyloglucan with xyloglucan (XG), xyloglucan heptasaccharide (XXXG), guar galactomannan (GG) and cellohexaose (Cello) in the soluble phase at 25 μg/ml. Y axis represents the percentage of inhibition achieved by the polysaccharides/haptens. Error bars: SD (n=3)

    Journal: FEBS letters

    Article Title: Recognition of xyloglucan by the crystalline cellulose-binding site of a family 3a carbohydrate-binding module

    doi: 10.1016/j.febslet.2015.07.009

    Figure Lengend Snippet: In vitro recognition of xyloglucan. A. ELISA analysis of Ct CBM3a cipA , Ct CBM3a cipA-M5 and LM15 binding to tamarind xyloglucan. B. Competitive-inhibition ELISAs of LM15 and Ct CBM3a cipA binding to immobilised xyloglucan with xyloglucan (XG), xyloglucan heptasaccharide (XXXG), guar galactomannan (GG) and cellohexaose (Cello) in the soluble phase at 25 μg/ml. Y axis represents the percentage of inhibition achieved by the polysaccharides/haptens. Error bars: SD (n=3)

    Article Snippet: After blocking with MP/PBS and washing, six ten-fold serial dilutions from 50 μg/ml of xyloglucan from tamarind seeds (P-XYGLN Megazyme), xyloglucan heptasaccharide (O-X3G4 Megazyme), guar galactomannan medium viscosity (P-GGMMV Megazyme) and cellohexaose (O-CHE Megazyme) haptens were prepared and 50 μl added to microtritre plate wells.

    Techniques: In Vitro, Enzyme-linked Immunosorbent Assay, Binding Assay, Inhibition

    27 Al-NMR Profile of AlCl 3 in the Presence of Citrate and Xyloglucan.

    Journal: The Plant Cell

    Article Title: XTH31, Encoding an in Vitro XEH/XET-Active Enzyme, Regulates Aluminum Sensitivity by Modulating in Vivo XET Action, Cell Wall Xyloglucan Content, and Aluminum Binding Capacity in Arabidopsis [W]

    doi: 10.1105/tpc.112.106039

    Figure Lengend Snippet: 27 Al-NMR Profile of AlCl 3 in the Presence of Citrate and Xyloglucan.

    Article Snippet: The reaction mixture contained 100 μL of the enzyme extract (containing ∼40 µg protein), 0.4 mg mL−1 xyloglucan (Megazyme International), 0.2 mg mL−1 (∼150 µM) xyloglucan oligosaccharides (Megazyme International), and 0.1 M sodium phosphate buffer, pH 6, in a final volume of 200 µL.

    Techniques: Nuclear Magnetic Resonance

    Analysis of the Relative Abundance of Xyloglucan Oligosaccharides Released by Xyloglucanase.

    Journal: The Plant Cell

    Article Title: XTH31, Encoding an in Vitro XEH/XET-Active Enzyme, Regulates Aluminum Sensitivity by Modulating in Vivo XET Action, Cell Wall Xyloglucan Content, and Aluminum Binding Capacity in Arabidopsis [W]

    doi: 10.1105/tpc.112.106039

    Figure Lengend Snippet: Analysis of the Relative Abundance of Xyloglucan Oligosaccharides Released by Xyloglucanase.

    Article Snippet: The reaction mixture contained 100 μL of the enzyme extract (containing ∼40 µg protein), 0.4 mg mL−1 xyloglucan (Megazyme International), 0.2 mg mL−1 (∼150 µM) xyloglucan oligosaccharides (Megazyme International), and 0.1 M sodium phosphate buffer, pH 6, in a final volume of 200 µL.

    Techniques:

    Expression and activity of XTH . a . Expression of Nicotiana tabacum xyloglucan endotransglycosylase (XTH, Genbank Acc AB017025.1 ) in Vvpgip1 lines 37 and 45 relative to the untransformed control (WT). Standard deviation of the mean relative expression of four technical repeats per plant line is shown with error bars . b . Total XTH activity in tobacco leaves determined by a dot-blot enzyme activity assay. Leaves representing leaf position 3 was used for the assay. A two-tailed Student's t-test showed that p

    Journal: BMC Research Notes

    Article Title: Constitutive expression of a grapevine polygalacturonase-inhibiting protein affects gene expression and cell wall properties in uninfected tobacco

    doi: 10.1186/1756-0500-4-493

    Figure Lengend Snippet: Expression and activity of XTH . a . Expression of Nicotiana tabacum xyloglucan endotransglycosylase (XTH, Genbank Acc AB017025.1 ) in Vvpgip1 lines 37 and 45 relative to the untransformed control (WT). Standard deviation of the mean relative expression of four technical repeats per plant line is shown with error bars . b . Total XTH activity in tobacco leaves determined by a dot-blot enzyme activity assay. Leaves representing leaf position 3 was used for the assay. A two-tailed Student's t-test showed that p

    Article Snippet: Whatman 3MM paper was coated with 1% (w/v) Tamarind seed xyloglucan (Megazyme) dissolved in aqueous 0.5% (w/v) 1,1,1-trichloro-2-methylpropan-2-ol (Sigma-Aldrich, Steinheim, Germany).

    Techniques: Expressing, Activity Assay, Standard Deviation, Dot Blot, Enzyme Activity Assay, Two Tailed Test

    (WT) and all xxt mutant plants using selected xyloglucan-directed antibodies. Toluidine blue-stained sections of wild-type and

    Journal: Plant Physiology

    Article Title: Mutations in Multiple XXT Genes of Arabidopsis Reveal the Complexity of Xyloglucan Biosynthesis 1 Genes of Arabidopsis Reveal the Complexity of Xyloglucan Biosynthesis 1 [W] Genes of Arabidopsis Reveal the Complexity of Xyloglucan Biosynthesis 1 [W] [OA]

    doi: 10.1104/pp.112.198119

    Figure Lengend Snippet: (WT) and all xxt mutant plants using selected xyloglucan-directed antibodies. Toluidine blue-stained sections of wild-type and

    Article Snippet: -pulsed-amperometric detection of the oligosaccharides generated after Driselase treatment was performed on an ICS system (Dionex) equipped with a gradient pump, pulse-amperometric detector, and a CarboPac PA1 column. and xylan disaccharides were separated using a gradient that ranged from 0.1 n NaOH (A) to 100 m m Na-acetate in 0.1 n NaOH (B) at 1 mL min−1 under the following conditions: 0 to 15 min, 100% A; 15 to 40 min, from 0% to 100% B. Xyloglucan from tamarind ( Tamarindus indica ) seeds (Megazyme) treated with Driselase under the same conditions was used as a control.

    Techniques: Mutagenesis, Staining

    (WT) and all xxt mutant plants using selected xyloglucan-directed antibodies. Toluidine blue-stained sections of wild-type and mutant lines show the overall hypocotyl

    Journal: Plant Physiology

    Article Title: Mutations in Multiple XXT Genes of Arabidopsis Reveal the Complexity of Xyloglucan Biosynthesis 1 Genes of Arabidopsis Reveal the Complexity of Xyloglucan Biosynthesis 1 [W] Genes of Arabidopsis Reveal the Complexity of Xyloglucan Biosynthesis 1 [W] [OA]

    doi: 10.1104/pp.112.198119

    Figure Lengend Snippet: (WT) and all xxt mutant plants using selected xyloglucan-directed antibodies. Toluidine blue-stained sections of wild-type and mutant lines show the overall hypocotyl

    Article Snippet: -pulsed-amperometric detection of the oligosaccharides generated after Driselase treatment was performed on an ICS system (Dionex) equipped with a gradient pump, pulse-amperometric detector, and a CarboPac PA1 column. and xylan disaccharides were separated using a gradient that ranged from 0.1 n NaOH (A) to 100 m m Na-acetate in 0.1 n NaOH (B) at 1 mL min−1 under the following conditions: 0 to 15 min, 100% A; 15 to 40 min, from 0% to 100% B. Xyloglucan from tamarind ( Tamarindus indica ) seeds (Megazyme) treated with Driselase under the same conditions was used as a control.

    Techniques: Mutagenesis, Staining

    (WT) and all xxt mutant plants using selected xyloglucan-directed antibodies. Toluidine blue-stained sections of wild-type and mutant lines show

    Journal: Plant Physiology

    Article Title: Mutations in Multiple XXT Genes of Arabidopsis Reveal the Complexity of Xyloglucan Biosynthesis 1 Genes of Arabidopsis Reveal the Complexity of Xyloglucan Biosynthesis 1 [W] Genes of Arabidopsis Reveal the Complexity of Xyloglucan Biosynthesis 1 [W] [OA]

    doi: 10.1104/pp.112.198119

    Figure Lengend Snippet: (WT) and all xxt mutant plants using selected xyloglucan-directed antibodies. Toluidine blue-stained sections of wild-type and mutant lines show

    Article Snippet: -pulsed-amperometric detection of the oligosaccharides generated after Driselase treatment was performed on an ICS system (Dionex) equipped with a gradient pump, pulse-amperometric detector, and a CarboPac PA1 column. and xylan disaccharides were separated using a gradient that ranged from 0.1 n NaOH (A) to 100 m m Na-acetate in 0.1 n NaOH (B) at 1 mL min−1 under the following conditions: 0 to 15 min, 100% A; 15 to 40 min, from 0% to 100% B. Xyloglucan from tamarind ( Tamarindus indica ) seeds (Megazyme) treated with Driselase under the same conditions was used as a control.

    Techniques: Mutagenesis, Staining

    pH and temperature dependence and kinetic parameters of AtXTH3-mediated transglycosylation reaction. ( a ) pH (left) and temperature (right) dependence of AtXTH3-mediated transglycosylation (donor: amorphous cellulose; acceptor: aminopyridyl cellotetraose, GGGG -AP). ( b ) Michaelis constant ( K M ) and turnover number ( k cat ) for acceptor oligosaccharides (left: GGGG -AP; right: XXXG -AP) with amorphous cellulose as the donor substrate. ( c ) Michaelis constant and turnover number for donor substrates (left: cellulose donor and GGGG -AP acceptor; right: xyloglucan donor and XXXG -AP acceptor). The data are presented as the mean ± s.d. from three independent experiments. Different letters in ( a ) denote significant differences as determined by Tukey’s test ( p

    Journal: Scientific Reports

    Article Title: The plant cell-wall enzyme AtXTH3 catalyses covalent cross-linking between cellulose and cello-oligosaccharide

    doi: 10.1038/srep46099

    Figure Lengend Snippet: pH and temperature dependence and kinetic parameters of AtXTH3-mediated transglycosylation reaction. ( a ) pH (left) and temperature (right) dependence of AtXTH3-mediated transglycosylation (donor: amorphous cellulose; acceptor: aminopyridyl cellotetraose, GGGG -AP). ( b ) Michaelis constant ( K M ) and turnover number ( k cat ) for acceptor oligosaccharides (left: GGGG -AP; right: XXXG -AP) with amorphous cellulose as the donor substrate. ( c ) Michaelis constant and turnover number for donor substrates (left: cellulose donor and GGGG -AP acceptor; right: xyloglucan donor and XXXG -AP acceptor). The data are presented as the mean ± s.d. from three independent experiments. Different letters in ( a ) denote significant differences as determined by Tukey’s test ( p

    Article Snippet: Cello-oligosaccharides, laminaritetraose, and xyloglucan oligosaccharides (Seikagaku) were used as supplied or coupled with 2-aminopyridine as described previously .

    Techniques:

    Substrate specificity of AtXTH3. ( a ) Transglycosylation activity from amorphous cellulose (top) or xyloglucan (bottom) to aminopyridyl (AP) oligosaccharides (L 4 : laminaritetraose; C 4 : cellotetraose; X 7 : xyloglucan-heptasaccharide, XXXG ; X 9 : xyloglucan-nonasaccharide, XLLG ). ( b ) Comparison of the donor substrate preference during AtXTH3-mediated endotransglucosylation of cellulose preparations of different crystallinity. X 7 was used as the acceptor substrate. In ( a ) and ( b ), the data are presented as the mean ± s.d. from three independent experiments, and different letters denote significant differences as determined by Tukey’s test ( p

    Journal: Scientific Reports

    Article Title: The plant cell-wall enzyme AtXTH3 catalyses covalent cross-linking between cellulose and cello-oligosaccharide

    doi: 10.1038/srep46099

    Figure Lengend Snippet: Substrate specificity of AtXTH3. ( a ) Transglycosylation activity from amorphous cellulose (top) or xyloglucan (bottom) to aminopyridyl (AP) oligosaccharides (L 4 : laminaritetraose; C 4 : cellotetraose; X 7 : xyloglucan-heptasaccharide, XXXG ; X 9 : xyloglucan-nonasaccharide, XLLG ). ( b ) Comparison of the donor substrate preference during AtXTH3-mediated endotransglucosylation of cellulose preparations of different crystallinity. X 7 was used as the acceptor substrate. In ( a ) and ( b ), the data are presented as the mean ± s.d. from three independent experiments, and different letters denote significant differences as determined by Tukey’s test ( p

    Article Snippet: Cello-oligosaccharides, laminaritetraose, and xyloglucan oligosaccharides (Seikagaku) were used as supplied or coupled with 2-aminopyridine as described previously .

    Techniques: Activity Assay

    Characterization of AtXTH3 transglycosylation products. ( a ) LC/ESI-TOF mass spectra of reaction products generated in the course of AtXTH3-mediated transglycosylation (top: denatured; bottom: native) using cellohexaose ( GGGGGG ) as the donor substrate, and aminopyridyl cellotetraose ( GGGG -AP) (left) or xyloglucan-heptasaccharide ( XXXG -AP) (right) as the acceptor substrate. Two major peaks specifically detected in each native AtXTH3 preparation are annotated. The letters in green represent the structure of the donor substrate and its moiety transferred to the acceptor. The assay conditions for all reactions were set to remove the majority of the donor and acceptor substrates, although a fraction (less than 10%) of the acceptor remained (*1: [ XXXG -AP + H] + ; *2: [ XXXG -AP + OAc + H] + ). ( b ) MALDI-TOF mass spectrum of insoluble products of the AtXTH3-mediated transglycosylation where aminopyridyl cellohexaose ( GGGGGG -AP) was the sole substrate. The numbers above peaks denote the degree of polymerization.

    Journal: Scientific Reports

    Article Title: The plant cell-wall enzyme AtXTH3 catalyses covalent cross-linking between cellulose and cello-oligosaccharide

    doi: 10.1038/srep46099

    Figure Lengend Snippet: Characterization of AtXTH3 transglycosylation products. ( a ) LC/ESI-TOF mass spectra of reaction products generated in the course of AtXTH3-mediated transglycosylation (top: denatured; bottom: native) using cellohexaose ( GGGGGG ) as the donor substrate, and aminopyridyl cellotetraose ( GGGG -AP) (left) or xyloglucan-heptasaccharide ( XXXG -AP) (right) as the acceptor substrate. Two major peaks specifically detected in each native AtXTH3 preparation are annotated. The letters in green represent the structure of the donor substrate and its moiety transferred to the acceptor. The assay conditions for all reactions were set to remove the majority of the donor and acceptor substrates, although a fraction (less than 10%) of the acceptor remained (*1: [ XXXG -AP + H] + ; *2: [ XXXG -AP + OAc + H] + ). ( b ) MALDI-TOF mass spectrum of insoluble products of the AtXTH3-mediated transglycosylation where aminopyridyl cellohexaose ( GGGGGG -AP) was the sole substrate. The numbers above peaks denote the degree of polymerization.

    Article Snippet: Cello-oligosaccharides, laminaritetraose, and xyloglucan oligosaccharides (Seikagaku) were used as supplied or coupled with 2-aminopyridine as described previously .

    Techniques: Generated

    AtXTH3 subsite mapping. ( a ) Comparison of AtXTH3-mediated transglycosylation activities and reaction products when different combinations of donor/acceptor substrate combinations were used. Cellotriose ( GGG ), cellotetraose ( GGGG ), cellopentaose ( GGGGG ), and cellohexaose ( GGGGGG ) were used as the donors. Aminopyridyl glucose ( G -AP), cellobiose ( GG -AP), cellotriose ( GGG -AP), cellotetraose ( GGGG -AP), and xyloglucan-heptasaccharide ( XXXG -AP) were used as the acceptors. The reaction products were separated by anion-exchange chromatography coupled with fluorescent detection. Each chromatogram is presented as the difference of chromatograms from reactions with native and heat-denatured enzymes. Arrowheads indicate acceptor elution volumes. Arrows indicate major transglycosylation products, whose putative structure is given on the right. The letters in green represent the structure of the donor substrate and its moiety transferred to the acceptor. ( b ) Schematic representation of the AtXTH3 subsite based on the data from ( a ). The 3D model was predicted using the PHYRE2 server 54 with the amino acid sequence of AtXTH3 as a query; the template, found on the server, was the crystallographic data (1UMZ 56 ) of PttXET16A, a hybrid aspen XTH protein.

    Journal: Scientific Reports

    Article Title: The plant cell-wall enzyme AtXTH3 catalyses covalent cross-linking between cellulose and cello-oligosaccharide

    doi: 10.1038/srep46099

    Figure Lengend Snippet: AtXTH3 subsite mapping. ( a ) Comparison of AtXTH3-mediated transglycosylation activities and reaction products when different combinations of donor/acceptor substrate combinations were used. Cellotriose ( GGG ), cellotetraose ( GGGG ), cellopentaose ( GGGGG ), and cellohexaose ( GGGGGG ) were used as the donors. Aminopyridyl glucose ( G -AP), cellobiose ( GG -AP), cellotriose ( GGG -AP), cellotetraose ( GGGG -AP), and xyloglucan-heptasaccharide ( XXXG -AP) were used as the acceptors. The reaction products were separated by anion-exchange chromatography coupled with fluorescent detection. Each chromatogram is presented as the difference of chromatograms from reactions with native and heat-denatured enzymes. Arrowheads indicate acceptor elution volumes. Arrows indicate major transglycosylation products, whose putative structure is given on the right. The letters in green represent the structure of the donor substrate and its moiety transferred to the acceptor. ( b ) Schematic representation of the AtXTH3 subsite based on the data from ( a ). The 3D model was predicted using the PHYRE2 server 54 with the amino acid sequence of AtXTH3 as a query; the template, found on the server, was the crystallographic data (1UMZ 56 ) of PttXET16A, a hybrid aspen XTH protein.

    Article Snippet: Cello-oligosaccharides, laminaritetraose, and xyloglucan oligosaccharides (Seikagaku) were used as supplied or coupled with 2-aminopyridine as described previously .

    Techniques: Chromatography, Sequencing

    The assessment of the quantitative fluorescence signal of xylan-1/xyloglucan by using the corrected total cell fluorescence method (CTCF) with combination of ANOVA statistics analyses. Yellow bars indicate mock-inoculated and PVY-infected cv. Irys (susceptible) potato plants at 10, 14 and 21 days post-inoculation. Green bars represent mock-inoculated and PVY-inoculated Sárpo Mira (resistant) potato plants at 7, 10 and 14 days post-inoculation. Mean values CTCFC were evaluated at the p

    Journal: International Journal of Molecular Sciences

    Article Title: Spatiotemporal Changes in Xylan-1/Xyloglucan and Xyloglucan Xyloglucosyl Transferase (XTH-Xet5) as a Step-In of Ultrastructural Cell Wall Remodelling in Potato–Potato Virus Y (PVYNTN) Hypersensitive and Susceptible Reaction

    doi: 10.3390/ijms19082287

    Figure Lengend Snippet: The assessment of the quantitative fluorescence signal of xylan-1/xyloglucan by using the corrected total cell fluorescence method (CTCF) with combination of ANOVA statistics analyses. Yellow bars indicate mock-inoculated and PVY-infected cv. Irys (susceptible) potato plants at 10, 14 and 21 days post-inoculation. Green bars represent mock-inoculated and PVY-inoculated Sárpo Mira (resistant) potato plants at 7, 10 and 14 days post-inoculation. Mean values CTCFC were evaluated at the p

    Article Snippet: After that the grids with leaf sections were treated for 1 h with gold-conjugated secondary antibody, with anti-rabbit 15 nm (Sigma-Aldrich, Warsaw, Poland) for XTH localisation or with 10 nm for xylan-1/xyloglucan detection (Sigma-Aldrich, Warsaw, Poland), rinsed for 5 min in PBS and then in distilled water.

    Techniques: Fluorescence, Infection

    Immunofluorescence localisation of xylan-1/xyloglucan in potato–PVY NTN incompatible interaction. ( A ) Green fluorescence signal of xyl-1 in xylem phloem elements, also in parenchyma of mock-inoculated potato Sárpo Mira leaf. Bar 50 µm. ( B ) Green fluorescence signal of xyl-1 in xylem tracheary elements ( * ) 7 days post-PVY NTN inoculation. Bar 20 µm. ( C ) Xyl-1/xyloglucan signal (*) in epidermis and xylem 10 days post-PVY NTN inoculation. Bar 20 µm. ( D ) Xyl-1/xyloglucan signal (*) in phloem ( * ) 14 days post-PVY NTN inoculation. Bar 20 µm. ( E ) Lack of green fluorescence signal when primary antibodies were omitted—control. Bar 20 µm. Ep—epidermis, Me—mesophyll, Pa—parenchyma cell, Ph—phloem, VB—vascular bundle, X—xylem.

    Journal: International Journal of Molecular Sciences

    Article Title: Spatiotemporal Changes in Xylan-1/Xyloglucan and Xyloglucan Xyloglucosyl Transferase (XTH-Xet5) as a Step-In of Ultrastructural Cell Wall Remodelling in Potato–Potato Virus Y (PVYNTN) Hypersensitive and Susceptible Reaction

    doi: 10.3390/ijms19082287

    Figure Lengend Snippet: Immunofluorescence localisation of xylan-1/xyloglucan in potato–PVY NTN incompatible interaction. ( A ) Green fluorescence signal of xyl-1 in xylem phloem elements, also in parenchyma of mock-inoculated potato Sárpo Mira leaf. Bar 50 µm. ( B ) Green fluorescence signal of xyl-1 in xylem tracheary elements ( * ) 7 days post-PVY NTN inoculation. Bar 20 µm. ( C ) Xyl-1/xyloglucan signal (*) in epidermis and xylem 10 days post-PVY NTN inoculation. Bar 20 µm. ( D ) Xyl-1/xyloglucan signal (*) in phloem ( * ) 14 days post-PVY NTN inoculation. Bar 20 µm. ( E ) Lack of green fluorescence signal when primary antibodies were omitted—control. Bar 20 µm. Ep—epidermis, Me—mesophyll, Pa—parenchyma cell, Ph—phloem, VB—vascular bundle, X—xylem.

    Article Snippet: After that the grids with leaf sections were treated for 1 h with gold-conjugated secondary antibody, with anti-rabbit 15 nm (Sigma-Aldrich, Warsaw, Poland) for XTH localisation or with 10 nm for xylan-1/xyloglucan detection (Sigma-Aldrich, Warsaw, Poland), rinsed for 5 min in PBS and then in distilled water.

    Techniques: Immunofluorescence, Fluorescence

    Immunofluorescence localisation of xylan-1/xyloglucan in potato–PVY NTN compatible interaction. ( A ) Green fluorescence signal of xyl-1 in xylem tracheary elements ( * ) of mock-inoculated potato leaf on longitudinal section (control). Bar 50 µm. ( B ) Green fluorescence of xyloglucan in vascular bundle (VB, * ) and in low intensity in mesophyll 10 days post-PVY NTN inoculation. Bar 20 µm. ( C ) Fluorescence of xyl-1/xyloglucan in vascular bundle (arrows, phloem and xylem) and spongy mesophyll cells 14 days post-PVY NTN inoculation. Lower intensity of signal in mesophyll. Bar 20 µm. ( D ) Strong signal of xyl-1/xyloglucan (arrows) in vascular bundle (phloem xylem) of both types of mesophyll. Strong reorganisation of tissues’ patterns 21 days post-virus inoculation. Bar 20 µm. ( E ) Lack of green fluorescence signal when primary antibodies were omitted–control. Bar 20 µm. Me—mesophyll, PMe—palisade mesophyll, SMe—spongy mesophyll cell, VB—vascular bundle, X—xylem.

    Journal: International Journal of Molecular Sciences

    Article Title: Spatiotemporal Changes in Xylan-1/Xyloglucan and Xyloglucan Xyloglucosyl Transferase (XTH-Xet5) as a Step-In of Ultrastructural Cell Wall Remodelling in Potato–Potato Virus Y (PVYNTN) Hypersensitive and Susceptible Reaction

    doi: 10.3390/ijms19082287

    Figure Lengend Snippet: Immunofluorescence localisation of xylan-1/xyloglucan in potato–PVY NTN compatible interaction. ( A ) Green fluorescence signal of xyl-1 in xylem tracheary elements ( * ) of mock-inoculated potato leaf on longitudinal section (control). Bar 50 µm. ( B ) Green fluorescence of xyloglucan in vascular bundle (VB, * ) and in low intensity in mesophyll 10 days post-PVY NTN inoculation. Bar 20 µm. ( C ) Fluorescence of xyl-1/xyloglucan in vascular bundle (arrows, phloem and xylem) and spongy mesophyll cells 14 days post-PVY NTN inoculation. Lower intensity of signal in mesophyll. Bar 20 µm. ( D ) Strong signal of xyl-1/xyloglucan (arrows) in vascular bundle (phloem xylem) of both types of mesophyll. Strong reorganisation of tissues’ patterns 21 days post-virus inoculation. Bar 20 µm. ( E ) Lack of green fluorescence signal when primary antibodies were omitted–control. Bar 20 µm. Me—mesophyll, PMe—palisade mesophyll, SMe—spongy mesophyll cell, VB—vascular bundle, X—xylem.

    Article Snippet: After that the grids with leaf sections were treated for 1 h with gold-conjugated secondary antibody, with anti-rabbit 15 nm (Sigma-Aldrich, Warsaw, Poland) for XTH localisation or with 10 nm for xylan-1/xyloglucan detection (Sigma-Aldrich, Warsaw, Poland), rinsed for 5 min in PBS and then in distilled water.

    Techniques: Immunofluorescence, Fluorescence

    Immunogold labelling of xylan-1/xyloglucan for potato–PVY NTN incompatible interaction. ( A ) Xylan-1/xyloglucan localisation (arrows) in cell wall, vacuole and in cytoplasm, also associated with membranes. Bar 0.5 µm ( B ) Xylan-1/xyloglucan localisation (arrows) in companion cells and sieve element of mock-inoculated potato Sárpo Mira leaf. Depositions are visible in the cell wall, vacuole and cytoplasm. Bar 0.5 µm ( C ) Xylan-1/xyloglucan deposition (arrow) in xylem tracheary element and xylem parenchyma seven days post-PVY inoculation. Bar 2 µm ( D ) Xylan-1/xyloglucan localisation (arrows) inside sieve element, also in cell wall and vacuole of phloem parenchyma cells seven days post-PVY NTN inoculation. Bar 1 µm ( E ) Deposition in vacuole with multivesicular bodies (*, MVB) 10 days past virus inoculation. Bar 1 µm ( F ) Xyloglucan localisation (arrows) closely related with cell wall plasmodesmata 14 days after PVY inoculation in palisade mesophyll cell. Bar 1 µm ( G ) Xyl-1 deposition (*) in cell wall and cytoplasm in collenchyma of potato Sárpo Mira leaf 14 days post virus inoculation. Bar 1 µm. ( H ) Lack of gold deposition in mesophyll of potato Sárpo Mira leaf–PVY NTN compatible interaction when primary antibodies were omitted (control). Bar 2 µm. Ch—chloroplast, CW—cell wall, MVB—multivesicular bodies, Pd—plasmodesmata, SE—sieve element, TGN—trans-Golgi network, X—xylem tracheary element, XP—xylem parenchyma.

    Journal: International Journal of Molecular Sciences

    Article Title: Spatiotemporal Changes in Xylan-1/Xyloglucan and Xyloglucan Xyloglucosyl Transferase (XTH-Xet5) as a Step-In of Ultrastructural Cell Wall Remodelling in Potato–Potato Virus Y (PVYNTN) Hypersensitive and Susceptible Reaction

    doi: 10.3390/ijms19082287

    Figure Lengend Snippet: Immunogold labelling of xylan-1/xyloglucan for potato–PVY NTN incompatible interaction. ( A ) Xylan-1/xyloglucan localisation (arrows) in cell wall, vacuole and in cytoplasm, also associated with membranes. Bar 0.5 µm ( B ) Xylan-1/xyloglucan localisation (arrows) in companion cells and sieve element of mock-inoculated potato Sárpo Mira leaf. Depositions are visible in the cell wall, vacuole and cytoplasm. Bar 0.5 µm ( C ) Xylan-1/xyloglucan deposition (arrow) in xylem tracheary element and xylem parenchyma seven days post-PVY inoculation. Bar 2 µm ( D ) Xylan-1/xyloglucan localisation (arrows) inside sieve element, also in cell wall and vacuole of phloem parenchyma cells seven days post-PVY NTN inoculation. Bar 1 µm ( E ) Deposition in vacuole with multivesicular bodies (*, MVB) 10 days past virus inoculation. Bar 1 µm ( F ) Xyloglucan localisation (arrows) closely related with cell wall plasmodesmata 14 days after PVY inoculation in palisade mesophyll cell. Bar 1 µm ( G ) Xyl-1 deposition (*) in cell wall and cytoplasm in collenchyma of potato Sárpo Mira leaf 14 days post virus inoculation. Bar 1 µm. ( H ) Lack of gold deposition in mesophyll of potato Sárpo Mira leaf–PVY NTN compatible interaction when primary antibodies were omitted (control). Bar 2 µm. Ch—chloroplast, CW—cell wall, MVB—multivesicular bodies, Pd—plasmodesmata, SE—sieve element, TGN—trans-Golgi network, X—xylem tracheary element, XP—xylem parenchyma.

    Article Snippet: After that the grids with leaf sections were treated for 1 h with gold-conjugated secondary antibody, with anti-rabbit 15 nm (Sigma-Aldrich, Warsaw, Poland) for XTH localisation or with 10 nm for xylan-1/xyloglucan detection (Sigma-Aldrich, Warsaw, Poland), rinsed for 5 min in PBS and then in distilled water.

    Techniques:

    Xyloglucan fragments, released from seedling cell walls by incubation with a xyloglucan-specific endo -glucanase, were separated on a CarboPac PA200 anion-exchange column. The peak areas of xyloglucan-specific fragments was compared between WT and mutant plants in five independent samples. A glucan size standard was separated under identical conditions, and the degree of Glc-polymerization ( DP ) is indicated in the numbers on the x-axes . The major xyloglucan peaks were assigned by comparison with tamarind xyloglucan standard fragments. Shorter fragments, which are less substituted with xylose, are overrepresented in ugd2,3 , whereas longer fragments are slightly underrepresented in ugd2,3 . Statistically significant data ( p

    Journal: The Journal of Biological Chemistry

    Article Title: Down-regulation of UDP-glucuronic Acid Biosynthesis Leads to Swollen Plant Cell Walls and Severe Developmental Defects Associated with Changes in Pectic Polysaccharides *

    doi: 10.1074/jbc.M111.255695

    Figure Lengend Snippet: Xyloglucan fragments, released from seedling cell walls by incubation with a xyloglucan-specific endo -glucanase, were separated on a CarboPac PA200 anion-exchange column. The peak areas of xyloglucan-specific fragments was compared between WT and mutant plants in five independent samples. A glucan size standard was separated under identical conditions, and the degree of Glc-polymerization ( DP ) is indicated in the numbers on the x-axes . The major xyloglucan peaks were assigned by comparison with tamarind xyloglucan standard fragments. Shorter fragments, which are less substituted with xylose, are overrepresented in ugd2,3 , whereas longer fragments are slightly underrepresented in ugd2,3 . Statistically significant data ( p

    Article Snippet: Xyloglucan fingerprints were generated with a xyloglucan-specific endo -glucanase (Novozyme) according to Lerouxel et al. ( ).

    Techniques: Incubation, Mutagenesis, Gas Chromatography

    Dot-blot screening for XET activity in total extracts from diverse plant organs. (a) XET assays in 96-well format, on paper impregnated with 0.3% xyloglucan + 5 μM XGO–SR; (b) control assays on paper impregnated with XGO–SR alone. Rows A–D and E–H show results with low- and high-salt extracts, respectively, from the plant organs listed on the right. The enzyme solutions (4 μl) were incubated on the papers for 13 h at 22 °C. (c) XET assays on paper impregnated with 0.3% xyloglucan + 5 μM XGO–SR. The enzyme extracts (low-salt buffer) were from parsley (P) or asparagus (A), and either undiluted (row ‘1’) or 2–8-fold diluted (rows ‘/2’ to ‘/8’); 4 μl was applied to the paper and incubated at 22 °C for 0.5, 1, 2, 4, 6 or 12 h, as indicated.

    Journal: Phytochemistry

    Article Title: Discovery of small molecule inhibitors of xyloglucan endotransglucosylase (XET) activity by high-throughput screening

    doi: 10.1016/j.phytochem.2015.06.016

    Figure Lengend Snippet: Dot-blot screening for XET activity in total extracts from diverse plant organs. (a) XET assays in 96-well format, on paper impregnated with 0.3% xyloglucan + 5 μM XGO–SR; (b) control assays on paper impregnated with XGO–SR alone. Rows A–D and E–H show results with low- and high-salt extracts, respectively, from the plant organs listed on the right. The enzyme solutions (4 μl) were incubated on the papers for 13 h at 22 °C. (c) XET assays on paper impregnated with 0.3% xyloglucan + 5 μM XGO–SR. The enzyme extracts (low-salt buffer) were from parsley (P) or asparagus (A), and either undiluted (row ‘1’) or 2–8-fold diluted (rows ‘/2’ to ‘/8’); 4 μl was applied to the paper and incubated at 22 °C for 0.5, 1, 2, 4, 6 or 12 h, as indicated.

    Article Snippet: 3.1 Comparison of screens The dot-blot screen, using paper-immobilised xyloglucan as donor substrate, proved simple and effective, allowing us to test over 4000 xenobiotics, manually, in about 10 days.

    Techniques: Dot Blot, Activity Assay, Incubation

    Representative dot-blot screens for inhibitors of parsley XET activity. The papers had been impregnated with 0.3% xyloglucan + generally about 5 μM XGO–SR (though the exact concentration varied, which accounts for the differences between papers in the fluorescence intensity of the XET products). Parsley enzyme extract (4 μl) containing a specific xenobiotic (200 μg/ml) was pipetted onto each station. After 2 h incubation under humid conditions, the papers were washed and fluorescent reaction products of XET activity were recorded. The results are shown here for the six plates (P1–P6) representing the EDI collection of xenobiotics.

    Journal: Phytochemistry

    Article Title: Discovery of small molecule inhibitors of xyloglucan endotransglucosylase (XET) activity by high-throughput screening

    doi: 10.1016/j.phytochem.2015.06.016

    Figure Lengend Snippet: Representative dot-blot screens for inhibitors of parsley XET activity. The papers had been impregnated with 0.3% xyloglucan + generally about 5 μM XGO–SR (though the exact concentration varied, which accounts for the differences between papers in the fluorescence intensity of the XET products). Parsley enzyme extract (4 μl) containing a specific xenobiotic (200 μg/ml) was pipetted onto each station. After 2 h incubation under humid conditions, the papers were washed and fluorescent reaction products of XET activity were recorded. The results are shown here for the six plates (P1–P6) representing the EDI collection of xenobiotics.

    Article Snippet: 3.1 Comparison of screens The dot-blot screen, using paper-immobilised xyloglucan as donor substrate, proved simple and effective, allowing us to test over 4000 xenobiotics, manually, in about 10 days.

    Techniques: Dot Blot, Activity Assay, Concentration Assay, Fluorescence, Incubation

    Transglucanase Action Products Formed In Vivo in E. fluviatile Tissues. (A) January tissue slices were fed with [ 3 H]XXXGol for 20 h, and its covalent incorporation into 6 M NaOH extractable hemicelluloses (xyloglucan or MLG; XET + MXE product) or alkali-inextractable cellulose (putative CXE product) was quantified (linear reaction range). Putative CXE products were then treated with TFA (2 M, 120°C, 1 h) and remaining insoluble 3 H (TFA residue) was reassayed (“deeply sequestered” cellulose–[ 3 H]XXXGol CXE products). (B) Sequential digestion of the TFA-resistant CXE product by lichenase (3 h), cellulase (3 × 3 h), cellulase + cellobiohydrolase (3 h), and 2× cellulase (24 and 48 h). (C) Thin-layer chromatography fingerprints of the digestion products formed from the TFA residues of in - vivo -generated cellulose–[ 3 H]XXXGol by in-vitro digestion with xyloglucan-inactive cellulase (EST, ESB, and GSB; pooled digests 3–5 from (B) ] and the subsequent synergic action of xyloglucan-inactive cellulase + cellobiohydrolase (EST, ESB, and GSB; digest 6). G n XXXGol, hybrid cello-oligosaccharide–xyloglucan heptasaccharide conjugate (where G n = number of glucose units in the cellulosic tail; n = 1–4). The structural diagram shows the expected sites of attack by “C” xyloglucan-inactive cellulose and, subsequently, “B” cellobiohydrolase. Purple arrows show the positions of markers; non-standard abbreviations: IP-ol, isoprimeveritol; Glc-ol, glucitol. (D and E) Similar experiment as in (A) ; however, MXE and XET action were distinguished by lichenase digestion of alkali-extracted hemicelluloses and expressed as amount of [ 3 H]XXXGol incorporated into the HTG products. XET, MXE, and CXE action were thus separately quantified in Equisetum tissues and P. annua (grass) leaves and stems ( n = 4, ±SD). In (D) , statistically significant differences ( p

    Journal: Molecular Plant

    Article Title: Hetero-trans-β-Glucanase Produces Cellulose–Xyloglucan Covalent Bonds in the Cell Walls of Structural Plant Tissues and Is Stimulated by Expansin

    doi: 10.1016/j.molp.2020.04.011

    Figure Lengend Snippet: Transglucanase Action Products Formed In Vivo in E. fluviatile Tissues. (A) January tissue slices were fed with [ 3 H]XXXGol for 20 h, and its covalent incorporation into 6 M NaOH extractable hemicelluloses (xyloglucan or MLG; XET + MXE product) or alkali-inextractable cellulose (putative CXE product) was quantified (linear reaction range). Putative CXE products were then treated with TFA (2 M, 120°C, 1 h) and remaining insoluble 3 H (TFA residue) was reassayed (“deeply sequestered” cellulose–[ 3 H]XXXGol CXE products). (B) Sequential digestion of the TFA-resistant CXE product by lichenase (3 h), cellulase (3 × 3 h), cellulase + cellobiohydrolase (3 h), and 2× cellulase (24 and 48 h). (C) Thin-layer chromatography fingerprints of the digestion products formed from the TFA residues of in - vivo -generated cellulose–[ 3 H]XXXGol by in-vitro digestion with xyloglucan-inactive cellulase (EST, ESB, and GSB; pooled digests 3–5 from (B) ] and the subsequent synergic action of xyloglucan-inactive cellulase + cellobiohydrolase (EST, ESB, and GSB; digest 6). G n XXXGol, hybrid cello-oligosaccharide–xyloglucan heptasaccharide conjugate (where G n = number of glucose units in the cellulosic tail; n = 1–4). The structural diagram shows the expected sites of attack by “C” xyloglucan-inactive cellulose and, subsequently, “B” cellobiohydrolase. Purple arrows show the positions of markers; non-standard abbreviations: IP-ol, isoprimeveritol; Glc-ol, glucitol. (D and E) Similar experiment as in (A) ; however, MXE and XET action were distinguished by lichenase digestion of alkali-extracted hemicelluloses and expressed as amount of [ 3 H]XXXGol incorporated into the HTG products. XET, MXE, and CXE action were thus separately quantified in Equisetum tissues and P. annua (grass) leaves and stems ( n = 4, ±SD). In (D) , statistically significant differences ( p

    Article Snippet: Xyloglucan endoglucanase was a gift from Novo Nordisk (Bagsværd, Denmark; ).

    Techniques: In Vivo, Thin Layer Chromatography, Generated, In Vitro

    Thin-Layer Chromatographic Profiling Diagnostic Fingerprints of In Vitro- Formed XET, MXE, and CXE Products. Polymer–[ 3 H]XXXGol conjugates, prepared enzymically in vitro , were digested with commercial enzymes and the products analyzed by thin-layer chromatography. Circled letters C, L, and X with heavy arrows indicate the expected sites of attack by xyloglucan-inactive cellulase, lichenase, and xyloglucan endoglucanase, respectively. Circled letters with faint arrows indicate unexpected sites of (slight) attack, possibly due to contaminating enzymes. (A) Markers were [ 3 H]XXXGol and [ 3 H]isoprimeveritol (IP-ol). Other profiles show the products formed from: the CXE product, cellulose–[ 3 H]XXXGol (B and C) ; the MXE product, MLG–[ 3 H]XXXGol (D–F) ; and the XET product, xyloglucan–[ 3 H]XXXGol (G–I) —by lichenase (D and G) , xyloglucan endoglucanase (B, E, and H) , or xyloglucan-inactive cellulase (C, F, and I) . On the structural diagrams, circle denotes glucose residue, star denotes xylose residue, and zigzag denotes [ 3 H]glucitol.

    Journal: Molecular Plant

    Article Title: Hetero-trans-β-Glucanase Produces Cellulose–Xyloglucan Covalent Bonds in the Cell Walls of Structural Plant Tissues and Is Stimulated by Expansin

    doi: 10.1016/j.molp.2020.04.011

    Figure Lengend Snippet: Thin-Layer Chromatographic Profiling Diagnostic Fingerprints of In Vitro- Formed XET, MXE, and CXE Products. Polymer–[ 3 H]XXXGol conjugates, prepared enzymically in vitro , were digested with commercial enzymes and the products analyzed by thin-layer chromatography. Circled letters C, L, and X with heavy arrows indicate the expected sites of attack by xyloglucan-inactive cellulase, lichenase, and xyloglucan endoglucanase, respectively. Circled letters with faint arrows indicate unexpected sites of (slight) attack, possibly due to contaminating enzymes. (A) Markers were [ 3 H]XXXGol and [ 3 H]isoprimeveritol (IP-ol). Other profiles show the products formed from: the CXE product, cellulose–[ 3 H]XXXGol (B and C) ; the MXE product, MLG–[ 3 H]XXXGol (D–F) ; and the XET product, xyloglucan–[ 3 H]XXXGol (G–I) —by lichenase (D and G) , xyloglucan endoglucanase (B, E, and H) , or xyloglucan-inactive cellulase (C, F, and I) . On the structural diagrams, circle denotes glucose residue, star denotes xylose residue, and zigzag denotes [ 3 H]glucitol.

    Article Snippet: Xyloglucan endoglucanase was a gift from Novo Nordisk (Bagsværd, Denmark; ).

    Techniques: Diagnostic Assay, In Vitro, Thin Layer Chromatography