{"title":"C1q与β 2微球蛋白的相互作用。","authors":"L Björck, U Johnson, A G Sjöholm","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Beta 2-microglobulin aggregated with glutaric dialdehyde was efficiently bound to C1q in fluid and solid phase assay systems. Furthermore, affinity chromatography experiments suggested reactivity of monomeric beta 2-microglobulin with C1q. In spite of its C1q binding capacity, the aggregated beta 2-microglobulin did not activate the C1 complex in serum. This however, might have been due to the mode of aggregation.</p>","PeriodicalId":77654,"journal":{"name":"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement","volume":"284 ","pages":"19-23"},"PeriodicalIF":0.0000,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Interaction of C1q with beta 2-microglobulin.\",\"authors\":\"L Björck, U Johnson, A G Sjöholm\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Beta 2-microglobulin aggregated with glutaric dialdehyde was efficiently bound to C1q in fluid and solid phase assay systems. Furthermore, affinity chromatography experiments suggested reactivity of monomeric beta 2-microglobulin with C1q. In spite of its C1q binding capacity, the aggregated beta 2-microglobulin did not activate the C1 complex in serum. This however, might have been due to the mode of aggregation.</p>\",\"PeriodicalId\":77654,\"journal\":{\"name\":\"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement\",\"volume\":\"284 \",\"pages\":\"19-23\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1984-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"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 pathologica, microbiologica, et immunologica Scandinavica. Supplement","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Beta 2-microglobulin aggregated with glutaric dialdehyde was efficiently bound to C1q in fluid and solid phase assay systems. Furthermore, affinity chromatography experiments suggested reactivity of monomeric beta 2-microglobulin with C1q. In spite of its C1q binding capacity, the aggregated beta 2-microglobulin did not activate the C1 complex in serum. This however, might have been due to the mode of aggregation.
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