{"title":"微绒毛结合亮氨酸芳基酰胺酶在蛋白质最终消化中的生理重要性。1. 大鼠肠道亮氨酸芳基酰胺酶和氨基三肽酶的纯化分离[j]。","authors":"M Friedrich, G Schenk, R Noack","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The membrane-bound leucine arylamidase of the microvilli of the rat small intestine was solubilized by Triton X-100 and purified by gel and ion-exchange chromatography. As compared to the mucosa homogenate, the purification factor was 135. The leucine arylamidase and aminotripeptidase of the microvilli cannot be separated by chromatography. The cytosomal portion of the aminopeptidase is devoid of leucine arylamidase activity.</p>","PeriodicalId":11281,"journal":{"name":"Die Nahrung","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Physiological importance of microvilli-bound leucine arylamidase in the final digestion of proteins. 1. Purification and isolation of intestinal leucine arylamidase and aminotripeptidase of rats].\",\"authors\":\"M Friedrich, G Schenk, R Noack\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The membrane-bound leucine arylamidase of the microvilli of the rat small intestine was solubilized by Triton X-100 and purified by gel and ion-exchange chromatography. As compared to the mucosa homogenate, the purification factor was 135. The leucine arylamidase and aminotripeptidase of the microvilli cannot be separated by chromatography. The cytosomal portion of the aminopeptidase is devoid of leucine arylamidase activity.</p>\",\"PeriodicalId\":11281,\"journal\":{\"name\":\"Die Nahrung\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1981-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Die Nahrung\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Die Nahrung","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[Physiological importance of microvilli-bound leucine arylamidase in the final digestion of proteins. 1. Purification and isolation of intestinal leucine arylamidase and aminotripeptidase of rats].
The membrane-bound leucine arylamidase of the microvilli of the rat small intestine was solubilized by Triton X-100 and purified by gel and ion-exchange chromatography. As compared to the mucosa homogenate, the purification factor was 135. The leucine arylamidase and aminotripeptidase of the microvilli cannot be separated by chromatography. The cytosomal portion of the aminopeptidase is devoid of leucine arylamidase activity.
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