{"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}
引用次数: 0
Abstract
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.