{"title":"猪肾酰化酶分离新方法。Co2+， Mn2+， Ni2+和Cd2+-酶的动力学[j]。","authors":"I Gilles, H G Löffler, F Schneider","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>A new procedure for the isolation of highly purified acylamino acid amidohydrolase from hog kidney is described which allows the preparation of the enzyme with a recovery of about 45%, a 200 fold purification and a spec. activity of 350-500 U. The essential Zn2+ of the enzyme was exchanged for Co2+, Ni2+, Mn2+ and Cd2+, and the kinetic parameters KM, kcat and kcat/KM of the different enzyme species for a series of acetyl-L-amino acids were determined.</p>","PeriodicalId":23914,"journal":{"name":"Zeitschrift fur Naturforschung. Section C, Biosciences","volume":"39 9-10","pages":"1017-20"},"PeriodicalIF":0.0000,"publicationDate":"1984-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[New isolation procedure for swine kidney acylase. Kinetics of Co2+, Mn2+, Ni2+ and Cd2+-enzymes].\",\"authors\":\"I Gilles, H G Löffler, F Schneider\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A new procedure for the isolation of highly purified acylamino acid amidohydrolase from hog kidney is described which allows the preparation of the enzyme with a recovery of about 45%, a 200 fold purification and a spec. activity of 350-500 U. The essential Zn2+ of the enzyme was exchanged for Co2+, Ni2+, Mn2+ and Cd2+, and the kinetic parameters KM, kcat and kcat/KM of the different enzyme species for a series of acetyl-L-amino acids were determined.</p>\",\"PeriodicalId\":23914,\"journal\":{\"name\":\"Zeitschrift fur Naturforschung. Section C, Biosciences\",\"volume\":\"39 9-10\",\"pages\":\"1017-20\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1984-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Zeitschrift fur Naturforschung. Section C, Biosciences\",\"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":"Zeitschrift fur Naturforschung. Section C, Biosciences","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[New isolation procedure for swine kidney acylase. Kinetics of Co2+, Mn2+, Ni2+ and Cd2+-enzymes].
A new procedure for the isolation of highly purified acylamino acid amidohydrolase from hog kidney is described which allows the preparation of the enzyme with a recovery of about 45%, a 200 fold purification and a spec. activity of 350-500 U. The essential Zn2+ of the enzyme was exchanged for Co2+, Ni2+, Mn2+ and Cd2+, and the kinetic parameters KM, kcat and kcat/KM of the different enzyme species for a series of acetyl-L-amino acids were determined.
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