{"title":"短芽孢杆菌α -乙酰乳酸脱羧酶的完整氨基酸序列。","authors":"I Svendsen, B R Jensen, M Ottesen","doi":"10.1007/BF02907185","DOIUrl":null,"url":null,"abstract":"<p><p>The complete amino acid sequence of acetolactate decarboxylase (EC 4.1.1.5) from Bacillus brevis has been determined by sequencing of the intact enzyme and of peptides obtained by cleavage with cyanogen bromide, Staphylococcus aureus V8 protease and trypsin, respectively. Determination of the C-terminal part was made by treatment with carboxypeptidases Y and M II. The enzyme has a molecular weight of 29,093 and consists of 260 amino acid residues arranged in a single peptide chain without disulphide bonds.</p>","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"54 4","pages":"157-63"},"PeriodicalIF":0.0000,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02907185","citationCount":"5","resultStr":"{\"title\":\"Complete amino acid sequence of alpha-acetolactate decarboxylase from Bacillus brevis.\",\"authors\":\"I Svendsen, B R Jensen, M Ottesen\",\"doi\":\"10.1007/BF02907185\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The complete amino acid sequence of acetolactate decarboxylase (EC 4.1.1.5) from Bacillus brevis has been determined by sequencing of the intact enzyme and of peptides obtained by cleavage with cyanogen bromide, Staphylococcus aureus V8 protease and trypsin, respectively. Determination of the C-terminal part was made by treatment with carboxypeptidases Y and M II. The enzyme has a molecular weight of 29,093 and consists of 260 amino acid residues arranged in a single peptide chain without disulphide bonds.</p>\",\"PeriodicalId\":9616,\"journal\":{\"name\":\"Carlsberg Research Communications\",\"volume\":\"54 4\",\"pages\":\"157-63\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1989-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1007/BF02907185\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Carlsberg Research Communications\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1007/BF02907185\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Carlsberg Research Communications","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/BF02907185","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Complete amino acid sequence of alpha-acetolactate decarboxylase from Bacillus brevis.
The complete amino acid sequence of acetolactate decarboxylase (EC 4.1.1.5) from Bacillus brevis has been determined by sequencing of the intact enzyme and of peptides obtained by cleavage with cyanogen bromide, Staphylococcus aureus V8 protease and trypsin, respectively. Determination of the C-terminal part was made by treatment with carboxypeptidases Y and M II. The enzyme has a molecular weight of 29,093 and consists of 260 amino acid residues arranged in a single peptide chain without disulphide bonds.
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