{"title":"巨芽孢杆菌葡萄糖脱氢酶自结合的超离心研究。","authors":"D Schubert, E Maurer, K Boss, G Pfleiderer","doi":"10.1515/bchm2.1984.365.2.1445","DOIUrl":null,"url":null,"abstract":"<p><p>The self-association of glucose dehydrogenase (beta-D-glucose:NAD(P) 1-oxidoreductase, EC 1.1.1.47) from Bacillus megaterium was studied by analytical ultracentrifugation. The pH and composition of the buffer used were such that, owing to a reversible partial dissociation of the tetrameric enzyme, enzyme activity was reduced. It was found that under these conditions the protein exists in a monomer/dimer/tetramer association equilibrium.</p>","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 12","pages":"1445-9"},"PeriodicalIF":0.0000,"publicationDate":"1984-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.2.1445","citationCount":"3","resultStr":"{\"title\":\"An ultracentrifuge study on the self-association of glucose dehydrogenase from Bacillus megaterium.\",\"authors\":\"D Schubert, E Maurer, K Boss, G Pfleiderer\",\"doi\":\"10.1515/bchm2.1984.365.2.1445\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The self-association of glucose dehydrogenase (beta-D-glucose:NAD(P) 1-oxidoreductase, EC 1.1.1.47) from Bacillus megaterium was studied by analytical ultracentrifugation. The pH and composition of the buffer used were such that, owing to a reversible partial dissociation of the tetrameric enzyme, enzyme activity was reduced. It was found that under these conditions the protein exists in a monomer/dimer/tetramer association equilibrium.</p>\",\"PeriodicalId\":13015,\"journal\":{\"name\":\"Hoppe-Seyler's Zeitschrift fur physiologische Chemie\",\"volume\":\"365 12\",\"pages\":\"1445-9\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1984-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.2.1445\",\"citationCount\":\"3\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Hoppe-Seyler's Zeitschrift fur physiologische Chemie\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1515/bchm2.1984.365.2.1445\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1515/bchm2.1984.365.2.1445","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 3
摘要
采用超离心法研究了巨芽孢杆菌中葡萄糖脱氢酶(β - d -葡萄糖:NAD(P) 1-氧化还原酶，EC 1.1.1.47)的自结合。所使用的缓冲液的pH和组成是这样的，由于四聚体酶的可逆部分解离，酶活性降低。结果表明，在这些条件下，该蛋白以单体/二聚体/四聚体的结合平衡存在。
An ultracentrifuge study on the self-association of glucose dehydrogenase from Bacillus megaterium.
The self-association of glucose dehydrogenase (beta-D-glucose:NAD(P) 1-oxidoreductase, EC 1.1.1.47) from Bacillus megaterium was studied by analytical ultracentrifugation. The pH and composition of the buffer used were such that, owing to a reversible partial dissociation of the tetrameric enzyme, enzyme activity was reduced. It was found that under these conditions the protein exists in a monomer/dimer/tetramer association equilibrium.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
