Both the high molecular weight and the low molecular weight variants of urinary Y-glutamyl transpeptidase, displayed transpeptidase (pH optimum 8.6) and autotrans-peptidase (pH optimum 9.4) activities. Iodoacetamide inhibited the transpeptidase activity more efficiently than the autotranspeptidase activity with respect to both variants of Y-glutamyl 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. © 1982 Indian Academy of Sciences.
CITATION STYLE
Rambabu, K., & Pattabiraman, T. N. (1982). Studies on the properties of the variants of gamma-glutamyl transpeptidase in human urine. Journal of Biosciences, 4(3), 287–294. https://doi.org/10.1007/BF02702741
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