{"title":"人红细胞中可能存在尿酸结合α -1- α -2球蛋白的研究。","authors":"J. O. Alvsaker","doi":"10.3109/rhe1.1970.16.issue-1-4.18","DOIUrl":null,"url":null,"abstract":"SummaryRecent investigations indicate that urate is partly transported through the erythrocyte membrane by a process which might involve a protein-carrier system. In the present work erythrocyte proteins have therefore been studied with special emphasis on the possible presence of the urate-binding alpha-1 — alpha-2 globulin. The erythrocytes were destroyed by freezing and thawing and the “ghosts” subsequently treated with desoxycholate or ultrasound. The three different protein fractions obtained were subjected to anion exchange chromatography on DEAE-Sephadex columns according to the procedure employed for isolating the urate-binding alpha-1 — alpha-2 globulin. In this way 10—14 different non-hemoglobin protein zones could be distinguished by vertical starch gel electrophoresis. None of these proteins, however, seemed to be identical to the urate-binding alpha-1 - alpha-2 globulin.","PeriodicalId":7146,"journal":{"name":"Acta rheumatologica Scandinavica","volume":"5 1","pages":"144-50"},"PeriodicalIF":0.0000,"publicationDate":"1970-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":"{\"title\":\"Studies on the possible presence of the urate-binding alpha-1-alpha-2 globulin in human erythrocytes.\",\"authors\":\"J. O. Alvsaker\",\"doi\":\"10.3109/rhe1.1970.16.issue-1-4.18\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"SummaryRecent investigations indicate that urate is partly transported through the erythrocyte membrane by a process which might involve a protein-carrier system. In the present work erythrocyte proteins have therefore been studied with special emphasis on the possible presence of the urate-binding alpha-1 — alpha-2 globulin. The erythrocytes were destroyed by freezing and thawing and the “ghosts” subsequently treated with desoxycholate or ultrasound. The three different protein fractions obtained were subjected to anion exchange chromatography on DEAE-Sephadex columns according to the procedure employed for isolating the urate-binding alpha-1 — alpha-2 globulin. In this way 10—14 different non-hemoglobin protein zones could be distinguished by vertical starch gel electrophoresis. None of these proteins, however, seemed to be identical to the urate-binding alpha-1 - alpha-2 globulin.\",\"PeriodicalId\":7146,\"journal\":{\"name\":\"Acta rheumatologica Scandinavica\",\"volume\":\"5 1\",\"pages\":\"144-50\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1970-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Acta rheumatologica Scandinavica\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3109/rhe1.1970.16.issue-1-4.18\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta rheumatologica Scandinavica","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3109/rhe1.1970.16.issue-1-4.18","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Studies on the possible presence of the urate-binding alpha-1-alpha-2 globulin in human erythrocytes.
SummaryRecent investigations indicate that urate is partly transported through the erythrocyte membrane by a process which might involve a protein-carrier system. In the present work erythrocyte proteins have therefore been studied with special emphasis on the possible presence of the urate-binding alpha-1 — alpha-2 globulin. The erythrocytes were destroyed by freezing and thawing and the “ghosts” subsequently treated with desoxycholate or ultrasound. The three different protein fractions obtained were subjected to anion exchange chromatography on DEAE-Sephadex columns according to the procedure employed for isolating the urate-binding alpha-1 — alpha-2 globulin. In this way 10—14 different non-hemoglobin protein zones could be distinguished by vertical starch gel electrophoresis. None of these proteins, however, seemed to be identical to the urate-binding alpha-1 - alpha-2 globulin.