H. Sakura , H. Kobayashi , S. Tsuruta , S. Mizutani
{"title":"Oxytocinase-like enzyme in an ovarian dysgerminoma: A placenta-specific protein","authors":"H. Sakura , H. Kobayashi , S. Tsuruta , S. Mizutani","doi":"10.1016/0006-2944(85)90111-5","DOIUrl":null,"url":null,"abstract":"<div><p>Aminopeptidase from dysgerminoma was purified and characterized using <span>l</span>-leucine-β-naphthylamide as substrate. The enzyme was resistant to puromycine, methionine, amastatin, bastatin, and EDTA, and it was heat labile at 60°C. The enzyme showed the same electrophoretic mobility as pregnant-patient serum oxytocinase CAP<sub>1</sub> on polyacrylamide gel electrophoresis. <em>K</em><sub><em>m</em></sub> value against <em>S</em>-benzylcysteine-<em>p</em>-nitroanilide was 4.2 × 10<sup>−4</sup><span>m</span>. Oxytocin and vasopressin competitively inhibited the enzyme activity. Molecular weight of the enzyme was estimated to be 80,000 by Sephadex G-200 column chromatography. These results suggest that aminopeptidase from dysgerminoma is an oxytocinase-like enzyme, a placenta-specific protein.</p></div>","PeriodicalId":8781,"journal":{"name":"Biochemical medicine","volume":"34 2","pages":"Pages 195-202"},"PeriodicalIF":0.0000,"publicationDate":"1985-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-2944(85)90111-5","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemical medicine","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0006294485901115","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 2
Abstract
Aminopeptidase from dysgerminoma was purified and characterized using l-leucine-β-naphthylamide as substrate. The enzyme was resistant to puromycine, methionine, amastatin, bastatin, and EDTA, and it was heat labile at 60°C. The enzyme showed the same electrophoretic mobility as pregnant-patient serum oxytocinase CAP1 on polyacrylamide gel electrophoresis. Km value against S-benzylcysteine-p-nitroanilide was 4.2 × 10−4m. Oxytocin and vasopressin competitively inhibited the enzyme activity. Molecular weight of the enzyme was estimated to be 80,000 by Sephadex G-200 column chromatography. These results suggest that aminopeptidase from dysgerminoma is an oxytocinase-like enzyme, a placenta-specific protein.
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