{"title":"牛铜蓝蛋白与红细胞的相互作用。","authors":"A C Fischer, C A Goode","doi":"10.1080/10826069408010089","DOIUrl":null,"url":null,"abstract":"<p><p>Binding of ceruloplasmin to bovine erythrocytes was investigated. The interaction was specific as demonstrated by more than 85% inhibition by excess ceruloplasmin protein. Binding was also inhibited by copper-nitrilotriacetate. The KD for both intact erythrocytes and solubilized ghost membranes was of the order of 10(-7) M. Using an affinity column a specific ceruloplasmin-binding protein was isolated from ghost membranes. The protein has an apparent molecular mass of 100,000 with subunits of 45 and 50 KDa.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"24 2","pages":"151-65"},"PeriodicalIF":0.0000,"publicationDate":"1994-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069408010089","citationCount":"1","resultStr":"{\"title\":\"Interaction of bovine ceruloplasmin with erythrocytes.\",\"authors\":\"A C Fischer, C A Goode\",\"doi\":\"10.1080/10826069408010089\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Binding of ceruloplasmin to bovine erythrocytes was investigated. The interaction was specific as demonstrated by more than 85% inhibition by excess ceruloplasmin protein. Binding was also inhibited by copper-nitrilotriacetate. The KD for both intact erythrocytes and solubilized ghost membranes was of the order of 10(-7) M. Using an affinity column a specific ceruloplasmin-binding protein was isolated from ghost membranes. The protein has an apparent molecular mass of 100,000 with subunits of 45 and 50 KDa.</p>\",\"PeriodicalId\":20391,\"journal\":{\"name\":\"Preparative biochemistry\",\"volume\":\"24 2\",\"pages\":\"151-65\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-05-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1080/10826069408010089\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Preparative biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1080/10826069408010089\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Preparative biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/10826069408010089","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Interaction of bovine ceruloplasmin with erythrocytes.
Binding of ceruloplasmin to bovine erythrocytes was investigated. The interaction was specific as demonstrated by more than 85% inhibition by excess ceruloplasmin protein. Binding was also inhibited by copper-nitrilotriacetate. The KD for both intact erythrocytes and solubilized ghost membranes was of the order of 10(-7) M. Using an affinity column a specific ceruloplasmin-binding protein was isolated from ghost membranes. The protein has an apparent molecular mass of 100,000 with subunits of 45 and 50 KDa.
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