iodoacetamide Ge Healthcare Search Results


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  • 99
    Millipore iodoacetamide
    Characterisation of SIP(F8)-SS-DM1 and IgG(F8)-SS-DM1. (A) Schematic representation of SIP(F8)-SS-DM1, IgG(F8)-SS-DM1 and of the DM1-SH drug. (B) Biochemical characterization of the products and of reaction intermediates by SDS-PAGE, size-exclusion chromatography and ESI-MS. The calculated masses of SIP(F8)-SS-DM1 and IgG(F8)-SS-DM1 are 39464 and 24218 Dalton, respectively. M = molecular weight marker. Lanes 1 and 2 represent unmodified antibody in non-reducing and reducing conditions, lane 3 the <t>iodoacetamide</t> conjugate, lane 4 the Ellman intermediate, lane 5 the final DM1 conjugate. (% I = % of MS signal intensity)
    Iodoacetamide, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 12698 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare dtt
    Analysis of glycoprotein turnover in TR- and ME-infected cells. nHDF were infected with 1 PFU/cell of TR or ME. At 5 dpi, infected cells were metabolically labeled with [ 35 S]cysteine-methionine for 15 min, and the label was then chased for 0, 10, 60, 180, or 360 min. Membrane proteins were extracted in 1% Triton X-100, adjusted to 2% <t>SDS–30</t> mM <t>DTT,</t> heated to 75°C for 10 min, cooled to room temperature, and then diluted 35-fold. Immunoprecipitation was performed with anti-gH and -gO (TR- or ME-specific) antibodies, and precipitated proteins were analyzed by SDS-PAGE. Band densities were determined relative to the 0-min chase time. Results shown are representative of data from 4 independent experiments.
    Dtt, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 18664 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare ipgphor
    2D-SDS-PAGE of S. flexneri 3a outer membrane proteins. 100 µg of crude preparation of the outer membrane proteins was precipitated with TCA. The pellet was washed with 12.5% TCA, acetone and air dried. The precipitate was dissolved in 125 µl of the sample buffer (pH 4–7). The IPG strip (11 cm) was soaked in the sample solution placed in the ceramic container provided with the <t>IPGphor</t> system. The first dimension of the electrophoretic separation was done according to the manufacturer’s recommendations. Proteins resolved on the buffer strip were reduced with DTT and alkylated with iodoacetamide. For the second dimension the IPG strip was placed over a vertical slab of 12.5% polyacrylamide gel prepared according to Laemmli [40] . Protein spots were visualized using the silver staining method as described by Shevchenko et al. [41] . Spots 13_1 and 13_2 were identified as OmpC and spot 13_3 as OmpA ( Table 2 ).
    Ipgphor, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 3391 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare ipg strips
    2D-SDS-PAGE of S. flexneri 3a outer membrane proteins. 100 µg of crude preparation of the outer membrane proteins was precipitated with TCA. The pellet was washed with 12.5% TCA, acetone and air dried. The precipitate was dissolved in 125 µl of the sample buffer (pH 4–7). The IPG strip (11 cm) was soaked in the sample solution placed in the ceramic container provided with the <t>IPGphor</t> system. The first dimension of the electrophoretic separation was done according to the manufacturer’s recommendations. Proteins resolved on the buffer strip were reduced with DTT and alkylated with iodoacetamide. For the second dimension the IPG strip was placed over a vertical slab of 12.5% polyacrylamide gel prepared according to Laemmli [40] . Protein spots were visualized using the silver staining method as described by Shevchenko et al. [41] . Spots 13_1 and 13_2 were identified as OmpC and spot 13_3 as OmpA ( Table 2 ).
    Ipg Strips, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 5984 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore dtt
    2D-SDS-PAGE of S. flexneri 3a outer membrane proteins. 100 µg of crude preparation of the outer membrane proteins was precipitated with TCA. The pellet was washed with 12.5% TCA, acetone and air dried. The precipitate was dissolved in 125 µl of the sample buffer (pH 4–7). The IPG strip (11 cm) was soaked in the sample solution placed in the ceramic container provided with the <t>IPGphor</t> system. The first dimension of the electrophoretic separation was done according to the manufacturer’s recommendations. Proteins resolved on the buffer strip were reduced with DTT and alkylated with iodoacetamide. For the second dimension the IPG strip was placed over a vertical slab of 12.5% polyacrylamide gel prepared according to Laemmli [40] . Protein spots were visualized using the silver staining method as described by Shevchenko et al. [41] . Spots 13_1 and 13_2 were identified as OmpC and spot 13_3 as OmpA ( Table 2 ).
    Dtt, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 36382 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare ipg buffer
    2D-SDS-PAGE of S. flexneri 3a outer membrane proteins. 100 µg of crude preparation of the outer membrane proteins was precipitated with TCA. The pellet was washed with 12.5% TCA, acetone and air dried. The precipitate was dissolved in 125 µl of the sample buffer (pH 4–7). The IPG strip (11 cm) was soaked in the sample solution placed in the ceramic container provided with the <t>IPGphor</t> system. The first dimension of the electrophoretic separation was done according to the manufacturer’s recommendations. Proteins resolved on the buffer strip were reduced with DTT and alkylated with iodoacetamide. For the second dimension the IPG strip was placed over a vertical slab of 12.5% polyacrylamide gel prepared according to Laemmli [40] . Protein spots were visualized using the silver staining method as described by Shevchenko et al. [41] . Spots 13_1 and 13_2 were identified as OmpC and spot 13_3 as OmpA ( Table 2 ).
    Ipg Buffer, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 3356 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore bugbuster protein extraction reagent
    2D-SDS-PAGE of S. flexneri 3a outer membrane proteins. 100 µg of crude preparation of the outer membrane proteins was precipitated with TCA. The pellet was washed with 12.5% TCA, acetone and air dried. The precipitate was dissolved in 125 µl of the sample buffer (pH 4–7). The IPG strip (11 cm) was soaked in the sample solution placed in the ceramic container provided with the <t>IPGphor</t> system. The first dimension of the electrophoretic separation was done according to the manufacturer’s recommendations. Proteins resolved on the buffer strip were reduced with DTT and alkylated with iodoacetamide. For the second dimension the IPG strip was placed over a vertical slab of 12.5% polyacrylamide gel prepared according to Laemmli [40] . Protein spots were visualized using the silver staining method as described by Shevchenko et al. [41] . Spots 13_1 and 13_2 were identified as OmpC and spot 13_3 as OmpA ( Table 2 ).
    Bugbuster Protein Extraction Reagent, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 4364 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Promega trypsin
    2D-SDS-PAGE of S. flexneri 3a outer membrane proteins. 100 µg of crude preparation of the outer membrane proteins was precipitated with TCA. The pellet was washed with 12.5% TCA, acetone and air dried. The precipitate was dissolved in 125 µl of the sample buffer (pH 4–7). The IPG strip (11 cm) was soaked in the sample solution placed in the ceramic container provided with the <t>IPGphor</t> system. The first dimension of the electrophoretic separation was done according to the manufacturer’s recommendations. Proteins resolved on the buffer strip were reduced with DTT and alkylated with iodoacetamide. For the second dimension the IPG strip was placed over a vertical slab of 12.5% polyacrylamide gel prepared according to Laemmli [40] . Protein spots were visualized using the silver staining method as described by Shevchenko et al. [41] . Spots 13_1 and 13_2 were identified as OmpC and spot 13_3 as OmpA ( Table 2 ).
    Trypsin, supplied by Promega, used in various techniques. Bioz Stars score: 96/100, based on 39092 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare ettan dalt ii system
    2D-SDS-PAGE of S. flexneri 3a outer membrane proteins. 100 µg of crude preparation of the outer membrane proteins was precipitated with TCA. The pellet was washed with 12.5% TCA, acetone and air dried. The precipitate was dissolved in 125 µl of the sample buffer (pH 4–7). The IPG strip (11 cm) was soaked in the sample solution placed in the ceramic container provided with the <t>IPGphor</t> system. The first dimension of the electrophoretic separation was done according to the manufacturer’s recommendations. Proteins resolved on the buffer strip were reduced with DTT and alkylated with iodoacetamide. For the second dimension the IPG strip was placed over a vertical slab of 12.5% polyacrylamide gel prepared according to Laemmli [40] . Protein spots were visualized using the silver staining method as described by Shevchenko et al. [41] . Spots 13_1 and 13_2 were identified as OmpC and spot 13_3 as OmpA ( Table 2 ).
    Ettan Dalt Ii System, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 631 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad iodoacetamide
    2D-SDS-PAGE of S. flexneri 3a outer membrane proteins. 100 µg of crude preparation of the outer membrane proteins was precipitated with TCA. The pellet was washed with 12.5% TCA, acetone and air dried. The precipitate was dissolved in 125 µl of the sample buffer (pH 4–7). The IPG strip (11 cm) was soaked in the sample solution placed in the ceramic container provided with the <t>IPGphor</t> system. The first dimension of the electrophoretic separation was done according to the manufacturer’s recommendations. Proteins resolved on the buffer strip were reduced with DTT and alkylated with iodoacetamide. For the second dimension the IPG strip was placed over a vertical slab of 12.5% polyacrylamide gel prepared according to Laemmli [40] . Protein spots were visualized using the silver staining method as described by Shevchenko et al. [41] . Spots 13_1 and 13_2 were identified as OmpC and spot 13_3 as OmpA ( Table 2 ).
    Iodoacetamide, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1118 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare 2 d quant kit
    Photosynthetic parameters. leaf net photosynthesis ( A ), leaf-to-air water vapour drawdown ( B ), leaf glucose content ( C ) and Gly-to-Ser ratio ( D ), under the different photosynthetic contexts used (LC, NC and HC: 100, 380 and 1000 µmol mol −1  CO 2 ; D: darkness).
    2 D Quant Kit, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 4658 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore ammonium bicarbonate
    Photosynthetic parameters. leaf net photosynthesis ( A ), leaf-to-air water vapour drawdown ( B ), leaf glucose content ( C ) and Gly-to-Ser ratio ( D ), under the different photosynthetic contexts used (LC, NC and HC: 100, 380 and 1000 µmol mol −1  CO 2 ; D: darkness).
    Ammonium Bicarbonate, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 5580 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad protean ief cell
    Photosynthetic parameters. leaf net photosynthesis ( A ), leaf-to-air water vapour drawdown ( B ), leaf glucose content ( C ) and Gly-to-Ser ratio ( D ), under the different photosynthetic contexts used (LC, NC and HC: 100, 380 and 1000 µmol mol −1  CO 2 ; D: darkness).
    Protean Ief Cell, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 5637 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    dtt  (Bio-Rad)
    99
    Bio-Rad dtt
    Photosynthetic parameters. leaf net photosynthesis ( A ), leaf-to-air water vapour drawdown ( B ), leaf glucose content ( C ) and Gly-to-Ser ratio ( D ), under the different photosynthetic contexts used (LC, NC and HC: 100, 380 and 1000 µmol mol −1  CO 2 ; D: darkness).
    Dtt, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 5935 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore tris
    Photosynthetic parameters. leaf net photosynthesis ( A ), leaf-to-air water vapour drawdown ( B ), leaf glucose content ( C ) and Gly-to-Ser ratio ( D ), under the different photosynthetic contexts used (LC, NC and HC: 100, 380 and 1000 µmol mol −1  CO 2 ; D: darkness).
    Tris, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 38479 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Characterisation of SIP(F8)-SS-DM1 and IgG(F8)-SS-DM1. (A) Schematic representation of SIP(F8)-SS-DM1, IgG(F8)-SS-DM1 and of the DM1-SH drug. (B) Biochemical characterization of the products and of reaction intermediates by SDS-PAGE, size-exclusion chromatography and ESI-MS. The calculated masses of SIP(F8)-SS-DM1 and IgG(F8)-SS-DM1 are 39464 and 24218 Dalton, respectively. M = molecular weight marker. Lanes 1 and 2 represent unmodified antibody in non-reducing and reducing conditions, lane 3 the iodoacetamide conjugate, lane 4 the Ellman intermediate, lane 5 the final DM1 conjugate. (% I = % of MS signal intensity)

    Journal: Molecular cancer therapeutics

    Article Title: Antibody format and drug release rate determine the therapeutic activity of non-internalizing antibody-drug conjugates

    doi: 10.1158/1535-7163.MCT-15-0480

    Figure Lengend Snippet: Characterisation of SIP(F8)-SS-DM1 and IgG(F8)-SS-DM1. (A) Schematic representation of SIP(F8)-SS-DM1, IgG(F8)-SS-DM1 and of the DM1-SH drug. (B) Biochemical characterization of the products and of reaction intermediates by SDS-PAGE, size-exclusion chromatography and ESI-MS. The calculated masses of SIP(F8)-SS-DM1 and IgG(F8)-SS-DM1 are 39464 and 24218 Dalton, respectively. M = molecular weight marker. Lanes 1 and 2 represent unmodified antibody in non-reducing and reducing conditions, lane 3 the iodoacetamide conjugate, lane 4 the Ellman intermediate, lane 5 the final DM1 conjugate. (% I = % of MS signal intensity)

    Article Snippet: The reaction was stopped after 5 min or 15 min for the antibodies in SIP or IgG format, respectively, by the addition of 500 equivalents (per antibody monomer) of a stock solution of iodoacetamide (Sigma Aldrich), dissolved in water at a concentration of 0.1 mM.

    Techniques: SDS Page, Size-exclusion Chromatography, Mass Spectrometry, Molecular Weight, Marker

    Analysis of glycoprotein turnover in TR- and ME-infected cells. nHDF were infected with 1 PFU/cell of TR or ME. At 5 dpi, infected cells were metabolically labeled with [ 35 S]cysteine-methionine for 15 min, and the label was then chased for 0, 10, 60, 180, or 360 min. Membrane proteins were extracted in 1% Triton X-100, adjusted to 2% SDS–30 mM DTT, heated to 75°C for 10 min, cooled to room temperature, and then diluted 35-fold. Immunoprecipitation was performed with anti-gH and -gO (TR- or ME-specific) antibodies, and precipitated proteins were analyzed by SDS-PAGE. Band densities were determined relative to the 0-min chase time. Results shown are representative of data from 4 independent experiments.

    Journal: Journal of Virology

    Article Title: Expression Levels of Glycoprotein O (gO) Vary between Strains of Human Cytomegalovirus, Influencing the Assembly of gH/gL Complexes and Virion Infectivity

    doi: 10.1128/JVI.00606-18

    Figure Lengend Snippet: Analysis of glycoprotein turnover in TR- and ME-infected cells. nHDF were infected with 1 PFU/cell of TR or ME. At 5 dpi, infected cells were metabolically labeled with [ 35 S]cysteine-methionine for 15 min, and the label was then chased for 0, 10, 60, 180, or 360 min. Membrane proteins were extracted in 1% Triton X-100, adjusted to 2% SDS–30 mM DTT, heated to 75°C for 10 min, cooled to room temperature, and then diluted 35-fold. Immunoprecipitation was performed with anti-gH and -gO (TR- or ME-specific) antibodies, and precipitated proteins were analyzed by SDS-PAGE. Band densities were determined relative to the 0-min chase time. Results shown are representative of data from 4 independent experiments.

    Article Snippet: Protein A-agarose beads were washed 3 times with TBS-TX-DOC, and proteins were eluted with 2% SDS and 30 mM DTT in TBS at room temperature (RT) for 15 min, followed by 75°C for 10 min. Eluted proteins were separated by SDS-PAGE and analyzed with a Typhoon FLA-9500 imager (GE Healthcare Life Sciences).

    Techniques: Infection, Metabolic Labelling, Labeling, Immunoprecipitation, SDS Page

    2D-SDS-PAGE of S. flexneri 3a outer membrane proteins. 100 µg of crude preparation of the outer membrane proteins was precipitated with TCA. The pellet was washed with 12.5% TCA, acetone and air dried. The precipitate was dissolved in 125 µl of the sample buffer (pH 4–7). The IPG strip (11 cm) was soaked in the sample solution placed in the ceramic container provided with the IPGphor system. The first dimension of the electrophoretic separation was done according to the manufacturer’s recommendations. Proteins resolved on the buffer strip were reduced with DTT and alkylated with iodoacetamide. For the second dimension the IPG strip was placed over a vertical slab of 12.5% polyacrylamide gel prepared according to Laemmli [40] . Protein spots were visualized using the silver staining method as described by Shevchenko et al. [41] . Spots 13_1 and 13_2 were identified as OmpC and spot 13_3 as OmpA ( Table 2 ).

    Journal: PLoS ONE

    Article Title: Shigella flexneri 3a Outer Membrane Protein C Epitope Is Recognized by Human Umbilical Cord Sera and Associated with Protective Activity

    doi: 10.1371/journal.pone.0070539

    Figure Lengend Snippet: 2D-SDS-PAGE of S. flexneri 3a outer membrane proteins. 100 µg of crude preparation of the outer membrane proteins was precipitated with TCA. The pellet was washed with 12.5% TCA, acetone and air dried. The precipitate was dissolved in 125 µl of the sample buffer (pH 4–7). The IPG strip (11 cm) was soaked in the sample solution placed in the ceramic container provided with the IPGphor system. The first dimension of the electrophoretic separation was done according to the manufacturer’s recommendations. Proteins resolved on the buffer strip were reduced with DTT and alkylated with iodoacetamide. For the second dimension the IPG strip was placed over a vertical slab of 12.5% polyacrylamide gel prepared according to Laemmli [40] . Protein spots were visualized using the silver staining method as described by Shevchenko et al. [41] . Spots 13_1 and 13_2 were identified as OmpC and spot 13_3 as OmpA ( Table 2 ).

    Article Snippet: The IEF was conducted in IPGphor (Amersham Pharmacia Biotech) at 15°C using a voltage step gradient as recommended by the manufacturer.

    Techniques: SDS Page, Stripping Membranes, Silver Staining

    Photosynthetic parameters. leaf net photosynthesis ( A ), leaf-to-air water vapour drawdown ( B ), leaf glucose content ( C ) and Gly-to-Ser ratio ( D ), under the different photosynthetic contexts used (LC, NC and HC: 100, 380 and 1000 µmol mol −1  CO 2 ; D: darkness).

    Journal: PLoS ONE

    Article Title: Photosynthetic Control of Arabidopsis Leaf Cytoplasmic Translation Initiation by Protein Phosphorylation

    doi: 10.1371/journal.pone.0070692

    Figure Lengend Snippet: Photosynthetic parameters. leaf net photosynthesis ( A ), leaf-to-air water vapour drawdown ( B ), leaf glucose content ( C ) and Gly-to-Ser ratio ( D ), under the different photosynthetic contexts used (LC, NC and HC: 100, 380 and 1000 µmol mol −1 CO 2 ; D: darkness).

    Article Snippet: Total protein content was determined using the 2-D Quant-kit (GE Healthcare).

    Techniques: