{"title":"Purification and properties of gamma-glutamyl transpeptidase from rat deciduoma.","authors":"U Tarachand","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>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.</p>","PeriodicalId":14978,"journal":{"name":"Journal of applied biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of applied biochemistry","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
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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