{"title":"Ultracentrifugal behavior of transferrin in the presence of some anions","authors":"Anatoly Bezkorovainy","doi":"10.1016/0926-6585(66)90065-3","DOIUrl":null,"url":null,"abstract":"<div><p>Transferrin of pooled human plasma has been found to aggregate reversibly in the presence of BrO<sub>3</sub><sup>−</sup>, IO<sub>3</sub><sup>−</sup>, SCN<sup>−</sup>, Cl<sup>−</sup>, Br<sup>−</sup>, I<sup>−</sup>, and NO<sub>3</sub><sup>−</sup>, giving weight-average sedimentation coefficients of from 5·50 S to 6·83 S compared to a normal <em>s</em><sub>20,<em>w</em></sub> of 5·10 S at 0·7% concentration. The aggregation was most pronounced in the vicinity of the isoelectric points of transferrin, <em>i.e.</em> at pH 5·0, and was dependent on the anion, but not on the protein concentration. No aggregation was observed in the presence of acetate, formate, chloroacetate, fluoride, cacodylate and sulfate at any pH value.</p></div>","PeriodicalId":100158,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","volume":"126 2","pages":"Pages 286-291"},"PeriodicalIF":0.0000,"publicationDate":"1966-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6585(66)90065-3","citationCount":"3","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926658566900653","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 3
Abstract
Transferrin of pooled human plasma has been found to aggregate reversibly in the presence of BrO3−, IO3−, SCN−, Cl−, Br−, I−, and NO3−, giving weight-average sedimentation coefficients of from 5·50 S to 6·83 S compared to a normal s20,w of 5·10 S at 0·7% concentration. The aggregation was most pronounced in the vicinity of the isoelectric points of transferrin, i.e. at pH 5·0, and was dependent on the anion, but not on the protein concentration. No aggregation was observed in the presence of acetate, formate, chloroacetate, fluoride, cacodylate and sulfate at any pH value.