{"title":"血浆纤维连接蛋白亚组分C1q结合位点的定位。","authors":"K B Reid, J Edmondson","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Previous studies on the interaction of fibronectin with C1q have yielded apparently conflicting results since both the globular head regions (produced by collagenase digestion) and the collagen-like domains (produced by limited pepsin digestion) have been reported to bind to fibronectin. In this study, the binding of 125I-labelled fibronectin to either intact C1q, or the collagenase or pepsin digestion products, immobilised on plastic microtitre plates was examined. Inhibition of the C1q-fibronectin interaction by the C1q digestion products was also examined. The results confirmed that both globular 'head' region preparations and collagen-like region preparations, can interact with fibronectin. Since the fragments used in these studies share a section of common amino acid sequence from the C1q molecule it can be concluded that the binding site, on C1q for fibronectin, is located in a region formed from the residues 81-97 of each of the three chains of the C1q molecule.</p>","PeriodicalId":77654,"journal":{"name":"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement","volume":"284 ","pages":"11-7"},"PeriodicalIF":0.0000,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Location of the binding site in subcomponent C1q for plasma fibronectin.\",\"authors\":\"K B Reid, J Edmondson\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Previous studies on the interaction of fibronectin with C1q have yielded apparently conflicting results since both the globular head regions (produced by collagenase digestion) and the collagen-like domains (produced by limited pepsin digestion) have been reported to bind to fibronectin. In this study, the binding of 125I-labelled fibronectin to either intact C1q, or the collagenase or pepsin digestion products, immobilised on plastic microtitre plates was examined. Inhibition of the C1q-fibronectin interaction by the C1q digestion products was also examined. The results confirmed that both globular 'head' region preparations and collagen-like region preparations, can interact with fibronectin. Since the fragments used in these studies share a section of common amino acid sequence from the C1q molecule it can be concluded that the binding site, on C1q for fibronectin, is located in a region formed from the residues 81-97 of each of the three chains of the C1q molecule.</p>\",\"PeriodicalId\":77654,\"journal\":{\"name\":\"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement\",\"volume\":\"284 \",\"pages\":\"11-7\"},\"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}
Location of the binding site in subcomponent C1q for plasma fibronectin.
Previous studies on the interaction of fibronectin with C1q have yielded apparently conflicting results since both the globular head regions (produced by collagenase digestion) and the collagen-like domains (produced by limited pepsin digestion) have been reported to bind to fibronectin. In this study, the binding of 125I-labelled fibronectin to either intact C1q, or the collagenase or pepsin digestion products, immobilised on plastic microtitre plates was examined. Inhibition of the C1q-fibronectin interaction by the C1q digestion products was also examined. The results confirmed that both globular 'head' region preparations and collagen-like region preparations, can interact with fibronectin. Since the fragments used in these studies share a section of common amino acid sequence from the C1q molecule it can be concluded that the binding site, on C1q for fibronectin, is located in a region formed from the residues 81-97 of each of the three chains of the C1q molecule.