Analysis of kinetic properties of gamma-glutamyl transpeptidase from rat kidney.
L Dvoráková, J Krůsek, F Stastný, V Lisý
Index: Gen. Physiol. Biophys. 15(5) , 403-13, (1996)
Full Text: HTML
Abstract
The initial rate kinetics of rat kidney gamma-glutamyl transpeptidase were measured using L-gamma-glutamyl-p-nitroanilide and glycyl-glycine as the donor and the acceptor substrate, respectively. Experimental data were fitted with the initial rate equation, and the obtained results indicated that: (1) Michaelis constants for transpeptidation (Kb), autotranspeptidation (Ka), and hydrolysis (Kh) are 8.56 mmol/l, 2.02 mmol/l and 0.005 mmol/l, respectively. (2) The maximum rate of transpeptidation (Vb) exceeds that of hydrolysis (Vh) and autotranspeptidation (Va) 160 times and 5 times, respectively. (3) A comparison of the ratios of maximal rate: Michaelis constant of individual reactions shows that hydrolysis is approximately 10 times more efficient than the remaining two reactions. (4) Under routine conditions used for gamma-glutamyl transpeptidase estimation, transpeptidation is the prevalent reaction.
Related Compounds
Related Articles:
2013-04-25
[Chem. Biol. Interact. 203(2) , 480-5, (2013)]
2015-05-01
[J. Steroid Biochem. Mol. Biol. 149 , 118-27, (2015)]
2012-06-01
[J. Food Sci. 77(6) , C640-5, (2012)]
2001-02-09
[Biochim. Biophys. Acta 1545(1-2) , 184-91, (2001)]
1998-09-01
[Eur. J. Biochem. 256(2) , 297-302, (1998)]