{"title":"哺乳动物组织的碱性(切割精氨酸和赖氨酸残基)金属羧肽酶:结构、性质和功能。","authors":"A N Vernigora, M T Gengin","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The structure, physical, chemical and catalitical properties, functions and biological role of mammalian basic carboxypeptidases are observing. On the strength of the genetic and filogenic research data it is supposed the existence of a family of basic metal-dependent carboxypeptidases and the plan of it evolution is proposed. The connections between structure, localisation and function of this enzyme are discussed.</p>","PeriodicalId":76775,"journal":{"name":"Ukrainskii biokhimicheskii zhurnal (1978)","volume":"70 4","pages":"16-24"},"PeriodicalIF":0.0000,"publicationDate":"1998-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Basic (cleaving arginine and lysine residues) metallocarboxypeptidase of mammalian tissue: structure, properties and function].\",\"authors\":\"A N Vernigora, M T Gengin\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The structure, physical, chemical and catalitical properties, functions and biological role of mammalian basic carboxypeptidases are observing. On the strength of the genetic and filogenic research data it is supposed the existence of a family of basic metal-dependent carboxypeptidases and the plan of it evolution is proposed. The connections between structure, localisation and function of this enzyme are discussed.</p>\",\"PeriodicalId\":76775,\"journal\":{\"name\":\"Ukrainskii biokhimicheskii zhurnal (1978)\",\"volume\":\"70 4\",\"pages\":\"16-24\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Ukrainskii biokhimicheskii zhurnal (1978)\",\"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":"Ukrainskii biokhimicheskii zhurnal (1978)","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[Basic (cleaving arginine and lysine residues) metallocarboxypeptidase of mammalian tissue: structure, properties and function].
The structure, physical, chemical and catalitical properties, functions and biological role of mammalian basic carboxypeptidases are observing. On the strength of the genetic and filogenic research data it is supposed the existence of a family of basic metal-dependent carboxypeptidases and the plan of it evolution is proposed. The connections between structure, localisation and function of this enzyme are discussed.
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