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  • 94
    Thermo Fisher iodoacetamide iam
    Iodoacetamide Iam, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore iodoacetamide iam
    Sensitivity of auto-ADP-ribosylation of TIPARP to different treatment conditions. ( A ) GST-TIPARP was incubated with different concentrations of MIBG for 5 min and auto-ribosylation was initiated with the addition of 32 P-NAD + as described in the Materials and Methods. ( B ) GST-TIPARP was incubated with 32 P-NAD + for 20 min at room temperature and then treated with 1 M neutral hydroxylamine (NH 2 OH) or NaCl for 1 or 2 h. ( C ) GST-TIPARP was incubated with different concentrations of <t>IAM</t> or 2 mM NaCl for 30 min at 37°C and the reaction was initiated with the addition of 32 P-NAD + as described in Materials and Methods. ADP-ribosylation was detected by autoradiography after SDS–PAGE followed by transfer onto a PVDF membrane. GCB staining shows levels of proteins loaded into SDS–PAGE gel. 3-ABA, 3-aminobemzamide. The data are representative of at least two independent experiments.
    Iodoacetamide Iam, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 366 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Bio-Rad iodoacetamide iam
    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of <t>iodoacetamide</t> (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed
    Iodoacetamide Iam, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 97/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    GE Healthcare iodoacetamide iam
    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of <t>iodoacetamide</t> (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed
    Iodoacetamide Iam, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 43 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Sinopharm iodoacetamide iam
    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of <t>iodoacetamide</t> (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed
    Iodoacetamide Iam, supplied by Sinopharm, used in various techniques. Bioz Stars score: 90/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Tokyo Chemical Industry iam iodoacetamide
    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of <t>iodoacetamide</t> (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed
    Iam Iodoacetamide, supplied by Tokyo Chemical Industry, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/iam iodoacetamide/product/Tokyo Chemical Industry
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    92
    Eppendorf AG iodoacetamide iam
    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of <t>iodoacetamide</t> (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed
    Iodoacetamide Iam, supplied by Eppendorf AG, used in various techniques. Bioz Stars score: 92/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Promega iodoacetamide iam
    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of <t>iodoacetamide</t> (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed
    Iodoacetamide Iam, supplied by Promega, used in various techniques. Bioz Stars score: 91/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore biotin iam
    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of <t>iodoacetamide</t> (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed
    Biotin Iam, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    OlChemIm n iam
    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of <t>iodoacetamide</t> (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed
    N Iam, supplied by OlChemIm, 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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    91
    Regis Technologies iam column
    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of <t>iodoacetamide</t> (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed
    Iam Column, supplied by Regis Technologies, 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
    Regis Technologies iam particles
    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of <t>iodoacetamide</t> (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed
    Iam Particles, supplied by Regis Technologies, 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
    Roche iodoacetomide iam
    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of <t>iodoacetamide</t> (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed
    Iodoacetomide Iam, supplied by Roche, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Sensitivity of auto-ADP-ribosylation of TIPARP to different treatment conditions. ( A ) GST-TIPARP was incubated with different concentrations of MIBG for 5 min and auto-ribosylation was initiated with the addition of 32 P-NAD + as described in the Materials and Methods. ( B ) GST-TIPARP was incubated with 32 P-NAD + for 20 min at room temperature and then treated with 1 M neutral hydroxylamine (NH 2 OH) or NaCl for 1 or 2 h. ( C ) GST-TIPARP was incubated with different concentrations of IAM or 2 mM NaCl for 30 min at 37°C and the reaction was initiated with the addition of 32 P-NAD + as described in Materials and Methods. ADP-ribosylation was detected by autoradiography after SDS–PAGE followed by transfer onto a PVDF membrane. GCB staining shows levels of proteins loaded into SDS–PAGE gel. 3-ABA, 3-aminobemzamide. The data are representative of at least two independent experiments.

    Journal: Biochemical Journal

    Article Title: Characterization of TCDD-inducible poly-ADP-ribose polymerase (TIPARP/ARTD14) catalytic activity

    doi: 10.1042/BCJ20180347

    Figure Lengend Snippet: Sensitivity of auto-ADP-ribosylation of TIPARP to different treatment conditions. ( A ) GST-TIPARP was incubated with different concentrations of MIBG for 5 min and auto-ribosylation was initiated with the addition of 32 P-NAD + as described in the Materials and Methods. ( B ) GST-TIPARP was incubated with 32 P-NAD + for 20 min at room temperature and then treated with 1 M neutral hydroxylamine (NH 2 OH) or NaCl for 1 or 2 h. ( C ) GST-TIPARP was incubated with different concentrations of IAM or 2 mM NaCl for 30 min at 37°C and the reaction was initiated with the addition of 32 P-NAD + as described in Materials and Methods. ADP-ribosylation was detected by autoradiography after SDS–PAGE followed by transfer onto a PVDF membrane. GCB staining shows levels of proteins loaded into SDS–PAGE gel. 3-ABA, 3-aminobemzamide. The data are representative of at least two independent experiments.

    Article Snippet: 3-Aminobenzoamide (3-ABA), ( N -(6-oxo-5,6-dihydrophenanthridin-2-yl)( N , N -dimethylamino) acetamide) (PJ34), meta-iodobenzylguanidine (MIBG), iodoacetamide (IAM), and NH2 OH (hydroxylamine) were purchased from Sigma-Aldrich (Oakville, Ontario).

    Techniques: Incubation, Autoradiography, SDS Page, Staining

    Formation of the μ1/μ1C ds bonds during the course of infection. T1L reovirus-infected cells were harvested at either 24, 48, 72, or 96 h postinfection. 50 mM IAM was added immediately upon resuspension of the infected cells in homogenization buffer. After purification, virions from each time point were mixed with nonreducing sample buffer (NR) and disrupted by boiling. The viral proteins were then resolved on a mini-sized SDS-8% PAGE gel. The amount of ds-bonded μ1/μ1C (% ds μ1/μ1C) relative to the total μ1, μ1C, and ds-bonded μ1/μ1C in each preparation was determined by densitometry of the Coomassie-stained gel. Immediately before harvesting, aliquots were taken from each time point and the proportion of dead/dying cells (% dead cells) was determined by trypan blue staining.

    Journal: Journal of Virology

    Article Title: Disulfide Bonding among ?1 Trimers in Mammalian Reovirus Outer Capsid: a Late and Reversible Step in Virion Morphogenesis

    doi: 10.1128/JVI.77.9.5389-5400.2003

    Figure Lengend Snippet: Formation of the μ1/μ1C ds bonds during the course of infection. T1L reovirus-infected cells were harvested at either 24, 48, 72, or 96 h postinfection. 50 mM IAM was added immediately upon resuspension of the infected cells in homogenization buffer. After purification, virions from each time point were mixed with nonreducing sample buffer (NR) and disrupted by boiling. The viral proteins were then resolved on a mini-sized SDS-8% PAGE gel. The amount of ds-bonded μ1/μ1C (% ds μ1/μ1C) relative to the total μ1, μ1C, and ds-bonded μ1/μ1C in each preparation was determined by densitometry of the Coomassie-stained gel. Immediately before harvesting, aliquots were taken from each time point and the proportion of dead/dying cells (% dead cells) was determined by trypan blue staining.

    Article Snippet: Iodoacetamide at a concentration of 50 mM (IAM; Sigma) was added during the course of some purifications as indicated in the legend to Fig. .

    Techniques: Infection, Homogenization, Purification, Polyacrylamide Gel Electrophoresis, Staining

    Analyses for ds bond formation with μ1 mutant C679S. (A) Recoated cores containing T1L wt σ3 and either T1L wt μ1 or the T1L μ1 mutant C679S were generated and purified, and particle concentrations were determined by densitometry. Equal amounts of the wt (lanes 2 and 5) or C679S (lanes 3 and 6) recoated cores were mixed with reducing (R) or nonreducing (NR) sample buffer, disrupted by boiling, and resolved on a mini-sized SDS-PAGE (8% acrylamide) gel. Virions disrupted under reducing (lane 1) or nonreducing (lane 4) conditions were included for comparison. Viral proteins were visualized by Coomassie staining. (B) Purified μ1-σ3 heterohexamers stored frozen in buffer with 10 mM DTT were thawed, and a small amount of each was diluted into nonreducing sample buffer and analyzed on a 4 to 15% acrylamide gradient native gel (Amersham Pharmacia Biotech) (lanes 1 to 3; 0 days). The remainder of each sample was passed through a PD-10 column to remove DTT and then stored at 4°C for 8 days at ambient conditions. At the end of that time, a small amount of each was diluted into sample buffer and analyzed on another 4 to 15% native gel (lanes 4 to 6). Three types of μ1-σ3 preparations were included in this analysis: complexes containing wt T1L μ1 and σ3 (lanes 1 and 4), complexes containing wt T1L μ1 and σ3 that were treated with 10 mM IAM to block free cysteines before storage (lanes 2 and 5), and complexes containing T1L C679S μ1 and wt T1L σ3 (lanes 3 and 6). The position of the native μ1-σ3 heterohexamer is indicated to the left. The positions of higher- M r forms specific to the complexes containing wt T1L μ1 and σ3 (lanes 1) are indicated (§). Positions of native gel markers (Amersham Pharmacia Biotech) are indicated in kilodaltons.

    Journal: Journal of Virology

    Article Title: Disulfide Bonding among ?1 Trimers in Mammalian Reovirus Outer Capsid: a Late and Reversible Step in Virion Morphogenesis

    doi: 10.1128/JVI.77.9.5389-5400.2003

    Figure Lengend Snippet: Analyses for ds bond formation with μ1 mutant C679S. (A) Recoated cores containing T1L wt σ3 and either T1L wt μ1 or the T1L μ1 mutant C679S were generated and purified, and particle concentrations were determined by densitometry. Equal amounts of the wt (lanes 2 and 5) or C679S (lanes 3 and 6) recoated cores were mixed with reducing (R) or nonreducing (NR) sample buffer, disrupted by boiling, and resolved on a mini-sized SDS-PAGE (8% acrylamide) gel. Virions disrupted under reducing (lane 1) or nonreducing (lane 4) conditions were included for comparison. Viral proteins were visualized by Coomassie staining. (B) Purified μ1-σ3 heterohexamers stored frozen in buffer with 10 mM DTT were thawed, and a small amount of each was diluted into nonreducing sample buffer and analyzed on a 4 to 15% acrylamide gradient native gel (Amersham Pharmacia Biotech) (lanes 1 to 3; 0 days). The remainder of each sample was passed through a PD-10 column to remove DTT and then stored at 4°C for 8 days at ambient conditions. At the end of that time, a small amount of each was diluted into sample buffer and analyzed on another 4 to 15% native gel (lanes 4 to 6). Three types of μ1-σ3 preparations were included in this analysis: complexes containing wt T1L μ1 and σ3 (lanes 1 and 4), complexes containing wt T1L μ1 and σ3 that were treated with 10 mM IAM to block free cysteines before storage (lanes 2 and 5), and complexes containing T1L C679S μ1 and wt T1L σ3 (lanes 3 and 6). The position of the native μ1-σ3 heterohexamer is indicated to the left. The positions of higher- M r forms specific to the complexes containing wt T1L μ1 and σ3 (lanes 1) are indicated (§). Positions of native gel markers (Amersham Pharmacia Biotech) are indicated in kilodaltons.

    Article Snippet: Iodoacetamide at a concentration of 50 mM (IAM; Sigma) was added during the course of some purifications as indicated in the legend to Fig. .

    Techniques: Mutagenesis, Generated, Purification, SDS Page, Acrylamide Gel Assay, Staining, Blocking Assay

    Effects of IAM addition on the migration of reovirus μ1 and μ1C proteins during SDS-PAGE. (A and B) Purified virions of reovirus T1L were used in these experiments. Viral proteins were resolved on a mini-sized SDS-PAGE [10% (A) or 8% (B) acrylamide] gel and visualized by Coomassie staining. The major new high- M r band observed after nonreducing disruption is indicated (*). (A) Virions were disrupted in sample buffer that contained no reducing agent (NR), and IAM was either not added (−) or added at different times after disruption (0 to 10 min) as indicated. (B) Virions were disrupted in pH 6.8 or 8.0 sample buffer that contained no reducing agent but to which 50 mM IAM was added either before (b) or immediately after (a) disruption as indicated. A sample of virions disrupted in reducing sample buffer (R; 5 mM DTT) was analyzed on the same gel (lane 1). Positions of molecular mass markers also resolved on the gel are indicated in kilodaltons. (C) Purified [ 35 S]methionine-cysteine-labeled virions of reovirus T3D were used in this experiment. The Coomassie-stained protein bands excised from the first gel (not shown; μ1C was obtained from samples of reduced virions and the high- M r band [*] was obtained from samples of IAM-treated nonreduced virions) were subjected to reduction in the gel fragments and otherwise treated as described in the text. The resulting proteins and protein fragments were resolved on a second gel and visualized by fluorography. The position of the full-length μ1C monomer is indicated. The amount of chymotrypsin added to each gel piece atop the second gel is also indicated. (D) Purified [ 35 S]methionine-cysteine- or [ 3 H]myristate-labeled virions of reovirus T3D were mixed with reducing or nonreducing sample buffer and disrupted in a boiling water bath. The viral proteins were then resolved on a full-sized 5 to 20% acrylamide gradient SDS-PAGE gel and visualized by fluorography. The major (*) and minor (**) new high- M r bands observed after nonreducing disruption of each sample are indicated.

    Journal: Journal of Virology

    Article Title: Disulfide Bonding among ?1 Trimers in Mammalian Reovirus Outer Capsid: a Late and Reversible Step in Virion Morphogenesis

    doi: 10.1128/JVI.77.9.5389-5400.2003

    Figure Lengend Snippet: Effects of IAM addition on the migration of reovirus μ1 and μ1C proteins during SDS-PAGE. (A and B) Purified virions of reovirus T1L were used in these experiments. Viral proteins were resolved on a mini-sized SDS-PAGE [10% (A) or 8% (B) acrylamide] gel and visualized by Coomassie staining. The major new high- M r band observed after nonreducing disruption is indicated (*). (A) Virions were disrupted in sample buffer that contained no reducing agent (NR), and IAM was either not added (−) or added at different times after disruption (0 to 10 min) as indicated. (B) Virions were disrupted in pH 6.8 or 8.0 sample buffer that contained no reducing agent but to which 50 mM IAM was added either before (b) or immediately after (a) disruption as indicated. A sample of virions disrupted in reducing sample buffer (R; 5 mM DTT) was analyzed on the same gel (lane 1). Positions of molecular mass markers also resolved on the gel are indicated in kilodaltons. (C) Purified [ 35 S]methionine-cysteine-labeled virions of reovirus T3D were used in this experiment. The Coomassie-stained protein bands excised from the first gel (not shown; μ1C was obtained from samples of reduced virions and the high- M r band [*] was obtained from samples of IAM-treated nonreduced virions) were subjected to reduction in the gel fragments and otherwise treated as described in the text. The resulting proteins and protein fragments were resolved on a second gel and visualized by fluorography. The position of the full-length μ1C monomer is indicated. The amount of chymotrypsin added to each gel piece atop the second gel is also indicated. (D) Purified [ 35 S]methionine-cysteine- or [ 3 H]myristate-labeled virions of reovirus T3D were mixed with reducing or nonreducing sample buffer and disrupted in a boiling water bath. The viral proteins were then resolved on a full-sized 5 to 20% acrylamide gradient SDS-PAGE gel and visualized by fluorography. The major (*) and minor (**) new high- M r bands observed after nonreducing disruption of each sample are indicated.

    Article Snippet: Iodoacetamide at a concentration of 50 mM (IAM; Sigma) was added during the course of some purifications as indicated in the legend to Fig. .

    Techniques: Migration, SDS Page, Purification, Acrylamide Gel Assay, Staining, Labeling

    Reversibility of the virion-associated μ1/μ1C ds bonds. For each experiment, aliquots were removed from the reaction mixture at the indicated intervals, and the reaction was quenched with 50 mM IAM. When all samples had been collected for each experiment, they were mixed with nonreducing sample buffer (NR) and disrupted by boiling. Viral proteins were resolved on mini-sized SDS-8% PAGE gels and visualized by Coomassie staining. (A) DTT at a concentration of 5 mM was added to purified T1L virions and allowed to incubate at room temperature to effect in situ reduction of the ds bonds. The 0-min aliquot (lane 1) was removed before the addition of DTT. Positions of molecular mass markers also resolved on the gel are indicated to the left. (B) The ds bonds in a sample of T1L virions were reduced by DTT as in panel A, lane 6, after which the DTT was removed by dialysis. Cystine at a concentration of 5 mM was then added to promote in situ reformation of the ds bonds. The 0-min aliquot (lane 1) was removed before the addition of cystine. A sample to which cysteine was never added was also analyzed (lane 9).

    Journal: Journal of Virology

    Article Title: Disulfide Bonding among ?1 Trimers in Mammalian Reovirus Outer Capsid: a Late and Reversible Step in Virion Morphogenesis

    doi: 10.1128/JVI.77.9.5389-5400.2003

    Figure Lengend Snippet: Reversibility of the virion-associated μ1/μ1C ds bonds. For each experiment, aliquots were removed from the reaction mixture at the indicated intervals, and the reaction was quenched with 50 mM IAM. When all samples had been collected for each experiment, they were mixed with nonreducing sample buffer (NR) and disrupted by boiling. Viral proteins were resolved on mini-sized SDS-8% PAGE gels and visualized by Coomassie staining. (A) DTT at a concentration of 5 mM was added to purified T1L virions and allowed to incubate at room temperature to effect in situ reduction of the ds bonds. The 0-min aliquot (lane 1) was removed before the addition of DTT. Positions of molecular mass markers also resolved on the gel are indicated to the left. (B) The ds bonds in a sample of T1L virions were reduced by DTT as in panel A, lane 6, after which the DTT was removed by dialysis. Cystine at a concentration of 5 mM was then added to promote in situ reformation of the ds bonds. The 0-min aliquot (lane 1) was removed before the addition of cystine. A sample to which cysteine was never added was also analyzed (lane 9).

    Article Snippet: Iodoacetamide at a concentration of 50 mM (IAM; Sigma) was added during the course of some purifications as indicated in the legend to Fig. .

    Techniques: Polyacrylamide Gel Electrophoresis, Staining, Concentration Assay, Purification, In Situ

    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of iodoacetamide (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed

    Journal: Plant Physiology

    Article Title: Glutamine Synthetase Is a Molecular Target of Nitric Oxide in Root Nodules of Medicago truncatula and Is Regulated by Tyrosine Nitration 1 and Is Regulated by Tyrosine Nitration 1 [W] and Is Regulated by Tyrosine Nitration 1 [W] [OA]

    doi: 10.1104/pp.111.186056

    Figure Lengend Snippet: Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of iodoacetamide (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed

    Article Snippet: TNM, S-GSNO, and SNP were obtained from Sigma; epicatechin and N -acetyl-imidazole were from Fluka; and iodocetamide was from Bio-Rad.

    Techniques: Activity Assay, Purification

    Effects of iodoacetamide on MtGS1a inactivation induced by TNM and PN. Purified MtGS1a was treated with 500 μ m iodoacetamide, followed by incubation with 50 μ m PN or 50 μ m TNM at pH 8, and assayed for GS activity. GS activity was

    Journal: Plant Physiology

    Article Title: Glutamine Synthetase Is a Molecular Target of Nitric Oxide in Root Nodules of Medicago truncatula and Is Regulated by Tyrosine Nitration 1 and Is Regulated by Tyrosine Nitration 1 [W] and Is Regulated by Tyrosine Nitration 1 [W] [OA]

    doi: 10.1104/pp.111.186056

    Figure Lengend Snippet: Effects of iodoacetamide on MtGS1a inactivation induced by TNM and PN. Purified MtGS1a was treated with 500 μ m iodoacetamide, followed by incubation with 50 μ m PN or 50 μ m TNM at pH 8, and assayed for GS activity. GS activity was

    Article Snippet: TNM, S-GSNO, and SNP were obtained from Sigma; epicatechin and N -acetyl-imidazole were from Fluka; and iodocetamide was from Bio-Rad.

    Techniques: Purification, Incubation, Activity Assay