{"title":"硬骨鱼肝精氨酸酶的纯化及性质研究。","authors":"R A Singh, S N Singh","doi":"10.3109/13813459009114003","DOIUrl":null,"url":null,"abstract":"<p><p>Liver arginase of Clarias batrachus has been purified to 56.3-fold employing ammonium sulphate fraction, DEAE-cellulose and CM-cellulose chromatography. Bidirectional polyacrylamide gel electrophoresis shows the presence of two isoenzymes of arginase. The enzyme has a molecular weight of about 87,000 and Km 15.38 mM for L-arginine, optimum pH 9.5 and temperature 37 degrees C. Ornithine and leucine as competitive whereas valine and isoleucine act as non-competitive inhibitors with respect to L-arginine as substrate.</p>","PeriodicalId":8170,"journal":{"name":"Archives internationales de physiologie et de biochimie","volume":"98 6","pages":"411-9"},"PeriodicalIF":0.0000,"publicationDate":"1990-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/13813459009114003","citationCount":"9","resultStr":"{\"title\":\"Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.).\",\"authors\":\"R A Singh, S N Singh\",\"doi\":\"10.3109/13813459009114003\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Liver arginase of Clarias batrachus has been purified to 56.3-fold employing ammonium sulphate fraction, DEAE-cellulose and CM-cellulose chromatography. Bidirectional polyacrylamide gel electrophoresis shows the presence of two isoenzymes of arginase. The enzyme has a molecular weight of about 87,000 and Km 15.38 mM for L-arginine, optimum pH 9.5 and temperature 37 degrees C. Ornithine and leucine as competitive whereas valine and isoleucine act as non-competitive inhibitors with respect to L-arginine as substrate.</p>\",\"PeriodicalId\":8170,\"journal\":{\"name\":\"Archives internationales de physiologie et de biochimie\",\"volume\":\"98 6\",\"pages\":\"411-9\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1990-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.3109/13813459009114003\",\"citationCount\":\"9\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Archives internationales de physiologie et de biochimie\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3109/13813459009114003\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Archives internationales de physiologie et de biochimie","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3109/13813459009114003","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.).
Liver arginase of Clarias batrachus has been purified to 56.3-fold employing ammonium sulphate fraction, DEAE-cellulose and CM-cellulose chromatography. Bidirectional polyacrylamide gel electrophoresis shows the presence of two isoenzymes of arginase. The enzyme has a molecular weight of about 87,000 and Km 15.38 mM for L-arginine, optimum pH 9.5 and temperature 37 degrees C. Ornithine and leucine as competitive whereas valine and isoleucine act as non-competitive inhibitors with respect to L-arginine as substrate.
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