Abstract
Summary A mixture of L -serine and borate is a potent competitive inhibitor of γ-glutamyl transpeptidase. Structural requirements for L -serine and the influence of some carbohydrates on this inhibition were investigated. Serine and borate can protect the enzyme against irreversible inactivation caused by iodoacetamide. The effect of pH and time of incubation with iodoacetamide, and the presence of an inhibitor on the rate of inactivation of the enzyme and on the rate of alkylation of cysteine, histidine, lysine and methionine was studied. Evidence is presented that glycollic acid liberated from alkylated γ-glutamyl transpeptidase by acid hydrolysis originates from the active center of the enzyme. Good agreement was obtained between the amount of purified γ-glutamyl transpeptidase (Fraction B) which liberated one mole of glycollic acid and the molecular weight of the enzyme.
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