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  • Title: Purification and properties of gamma-glutamyl transpeptidase from rat deciduoma.
    Author: Tarachand U.
    Journal: J Appl Biochem; 1984; 6(5-6):278-88. PubMed ID: 6152628.
    Abstract:
    gamma-Glutamyl transpeptidase has been purified by chromatographic methods from endometrium of rat deciduoma. The membrane-bound enzyme, digested with papain, eluted as a single fraction during chromatography and the final preparation had a specific activity of 104.5 U/mg protein. The molecular weight of the native enzyme was approximately 70,000 and the protein could be resolved into a heavy and a light fraction on sodium dodecyl sulfate-acrylamide gel electrophoresis with molecular weights of 45,000 and 23,000, respectively. The enzyme had a pH optimum of 8.2 and Km's for donor (p-nitroanilide) and acceptor (glycylglycine) were 1 and 7.6 mM, respectively. The enzyme was inhibited by L-serine in the presence of borate with a Ki of 22 microM. The decidual enzyme was not heat stable and its electrophoretic mobility was decreased after neuraminidase treatment.
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