PMID: 6113845Apr 14, 1981Paper

Some kinetic properties of gamma-glutamyltransferase from rabbit liver

Biochimica Et Biophysica Acta
D BagrelG Siest

Abstract

gamma-Glutamyltransferase ((5-glutamyl)-peptide: amino-acid 5-glutamyltransferase, EC 2.3.2.2) of rabbit liver (detergent form) was purified 1100-fold in order to study its kinetic properties. Kinetic studies were conducted from pH 6.0 to 12.0 in the absence and presence of the acceptor substrate glycylglycine using gamma-glutamyl-3-carboxy-4-nitroanilide as the donor. The existence of more than one binding site for both donor and acceptor is postulated on kinetic evidence such as donor substrate activation, donor substrate inhibition and acceptor substrate activation. Homotropic interaction is also observed, in the form of negative cooperativity, in donor substrate binding, in the absence of acceptor at pH less than 9.0 and positive cooperativity (n = 2), in the absence or presence of acceptor at pH greater than 9.0. Hydrolase reaction reaches a maximum of activity at pH 10 (pK 8.6). Transferase activity under conditions of maximal velocity is maximal at pH 9.0 (pK 7.1). The ratio of transferase activity/hydrolase activity is maximal at pH 7.0-7.5. At low donor substrate concentrations, maximal activity is attained at pH 7.5.

References

Oct 15, 1976·Clinica Chimica Acta; International Journal of Clinical Chemistry·L Theodorsen, J H Stromme
Jul 8, 1977·Biochimica Et Biophysica Acta·N E Huseby
Jul 3, 1978·European Journal of Biochemistry·S HoriuchiY Morino
May 11, 1971·European Journal of Biochemistry·M LazdunskiC Lazdunski
Sep 21, 2010·Blood·Shalini L ChudasamaGowthami M Arepally
Aug 16, 2011·Journal of Chromatography. a·Indu LathaQingping Tao

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Citations

May 5, 1981·Clinica Chimica Acta; International Journal of Clinical Chemistry·F SchieleG Siest
Nov 5, 1990·Clinica Chimica Acta; International Journal of Clinical Chemistry·A VisvikisG Siest
Nov 13, 2008·Archives of Biochemistry and Biophysics·Valeria AngeliEmilia Bramanti
Apr 11, 2014·TheScientificWorldJournal·Sharath Balakrishna, Asmita Prabhune

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