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Image Search Results
Journal: Analytical biochemistry
Article Title: Gamma-Glutamyl Compounds: Substrate Specificity of Gamma-Glutamyl Transpeptidase Enzymes
doi: 10.1016/j.ab.2011.03.026
Figure Lengend Snippet: Kinetic Analysis of GGT1 Substrate Specificity and Inhibition. (A) Double reciprocal plot of the initial velocity of GGT1 in the presence of GSH (●), GSSG (■), and LTC4 (▼). (B) Double reciprocal plot of the initial velocity versus substrate concentration in the presence of 0 mM (○), 0.625 mM (◆), 1.25 mM (▼), 2.5 mM (▲), 5 mM (■), and 10 mM (●) serine-borate. Data shown are average of triplicate values ± S.D. (For many points, the error bars are smaller than the symbol.) Enzyme was maintained at 10 mU.
Article Snippet: GGT Substrates and Inhibitor Stock solutions of glutathione (GSH, Sigma), oxidized glutathione (GSSG, Sigma), S-(4-Nitro-benzyl)glutathione (Sigma), S-methylglutathione (Sigma), glutathionesulfonic acid (Sigma), gamma-glutamyl leucine (Sigma), and
Techniques: Inhibition, Concentration Assay
Journal: Analytical biochemistry
Article Title: Gamma-Glutamyl Compounds: Substrate Specificity of Gamma-Glutamyl Transpeptidase Enzymes
doi: 10.1016/j.ab.2011.03.026
Figure Lengend Snippet: Kinetic Analysis of GGT5 Substrate Specificity and Inhibition. Double reciprocal plot of the initial velocities of human GGT5 versus substrate concentration: GSH (●), GSSG (■), and LTC4 (▼). Double reciprocal plot of the initial velocity of 10 mU GGT5 versus substrate concentration with 0 mM (○), 1.25 mM (◆), 2.5 mM (▼), 5 mM (▲), 10 mM (■), and 20 mM (●) serine-borate (B). Data shown are average of triplicate values ± S.D. (For many points, the error bars are smaller than the symbol.)
Article Snippet: GGT Substrates and Inhibitor Stock solutions of glutathione (GSH, Sigma), oxidized glutathione (GSSG, Sigma), S-(4-Nitro-benzyl)glutathione (Sigma), S-methylglutathione (Sigma), glutathionesulfonic acid (Sigma), gamma-glutamyl leucine (Sigma), and
Techniques: Inhibition, Concentration Assay