{"title":"人血清白蛋白中性转变的动力学","authors":"Jørgen Jacobsen, Thyge Faerch","doi":"10.1016/0005-2795(81)90056-8","DOIUrl":null,"url":null,"abstract":"<div><p>The fast step in the conformational change of human serum albumin from the alkaline to the neutral form of the albumin-bilirubin complex is studied by various pH jump experiments in a stopped-flow apparatus. The results indicate that the fast step is caused by electrostatic attraction between a carboxylate group of bilirubin and a histidine residue of albumin.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"670 1","pages":"Pages 124-128"},"PeriodicalIF":0.0000,"publicationDate":"1981-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90056-8","citationCount":"15","resultStr":"{\"title\":\"Kinetics of the neutral transition of human serum albumin\",\"authors\":\"Jørgen Jacobsen, Thyge Faerch\",\"doi\":\"10.1016/0005-2795(81)90056-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The fast step in the conformational change of human serum albumin from the alkaline to the neutral form of the albumin-bilirubin complex is studied by various pH jump experiments in a stopped-flow apparatus. The results indicate that the fast step is caused by electrostatic attraction between a carboxylate group of bilirubin and a histidine residue of albumin.</p></div>\",\"PeriodicalId\":100165,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Protein Structure\",\"volume\":\"670 1\",\"pages\":\"Pages 124-128\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1981-08-28\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0005-2795(81)90056-8\",\"citationCount\":\"15\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Protein Structure\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0005279581900568\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005279581900568","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Kinetics of the neutral transition of human serum albumin
The fast step in the conformational change of human serum albumin from the alkaline to the neutral form of the albumin-bilirubin complex is studied by various pH jump experiments in a stopped-flow apparatus. The results indicate that the fast step is caused by electrostatic attraction between a carboxylate group of bilirubin and a histidine residue of albumin.
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