Studies on the properties of the variants of gamma-glutamyl transpeptidase in human urine.
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Date
1982-09
Authors
Rambabu, K
Pattabiraman, T N
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Abstract
Both the high molecular weight and the low molecular weight variants of urinary
Y-glutamyl transpeptidase, displayed transpeptidase (pH optimum 8.6) and autotranspeptidase
(pH optimum 9.4) activities. Iodoacetamide inhibited the transpeptidase activity
more efficiently than the autotranspeptidase activity with respect to both variants of Yglutamyl
transpeptidase. The high molecular weight form utilized L-glutamine as a better
acceptor than L-cystine during the transpeptidation reaction whereas the reverse was the case
with the low molecular weight variant. While phenylmethylsulphonyl fluoride-treated
enzymes retained full activities per se, addition of maleic acid to the modified enzyme was
found to inhibit the catalytic activities indicating a maleic acid-induced conformational
change of the modified enzyme.
Description
Keywords
Urinary Y-glutamyl transpeptidase variants, autotranspeptidation, chemical modification
Citation
Rambabu K, Pattabiraman T N. Studies on the properties of the variants of gamma-glutamyl transpeptidase in human urine. Journal of Biosciences. 1982 Sept; 4(3): 287-294.