{"title":"人肾肾素的纯化。","authors":"E E Slater, R C Cohn, V J Dzau, E Haber","doi":"10.1042/cs055117s","DOIUrl":null,"url":null,"abstract":"<p><p>1. Human renal renin has been purified 200 000-fold from cadaver kidney cortex by a method which employs affinity chromatography on aminohexyl peptstatin. 2. The product of this purification has a specific activity of 400 Goldblatt units/mg when compared with Haas human renin standard. 3. This product appears as a single band on sodium dodecyl sulphate gel and polyacrylamide-disc gel electrophoresis. Renin enzymatic activity was recovered after elution from a polyacrylamide-disc gel run at pH 7.8. 4. Yield with this method was 1%.</p>","PeriodicalId":10672,"journal":{"name":"Clinical science and molecular medicine. Supplement","volume":"4 ","pages":"117s-119s"},"PeriodicalIF":0.0000,"publicationDate":"1978-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1042/cs055117s","citationCount":"19","resultStr":"{\"title\":\"Purification of human renal renin.\",\"authors\":\"E E Slater, R C Cohn, V J Dzau, E Haber\",\"doi\":\"10.1042/cs055117s\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>1. Human renal renin has been purified 200 000-fold from cadaver kidney cortex by a method which employs affinity chromatography on aminohexyl peptstatin. 2. The product of this purification has a specific activity of 400 Goldblatt units/mg when compared with Haas human renin standard. 3. This product appears as a single band on sodium dodecyl sulphate gel and polyacrylamide-disc gel electrophoresis. Renin enzymatic activity was recovered after elution from a polyacrylamide-disc gel run at pH 7.8. 4. Yield with this method was 1%.</p>\",\"PeriodicalId\":10672,\"journal\":{\"name\":\"Clinical science and molecular medicine. Supplement\",\"volume\":\"4 \",\"pages\":\"117s-119s\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1978-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1042/cs055117s\",\"citationCount\":\"19\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Clinical science and molecular medicine. Supplement\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1042/cs055117s\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Clinical science and molecular medicine. Supplement","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1042/cs055117s","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
1. Human renal renin has been purified 200 000-fold from cadaver kidney cortex by a method which employs affinity chromatography on aminohexyl peptstatin. 2. The product of this purification has a specific activity of 400 Goldblatt units/mg when compared with Haas human renin standard. 3. This product appears as a single band on sodium dodecyl sulphate gel and polyacrylamide-disc gel electrophoresis. Renin enzymatic activity was recovered after elution from a polyacrylamide-disc gel run at pH 7.8. 4. Yield with this method was 1%.
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