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.
No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong
Qilu Normal University · Genelibs Bioinformatics Lab
750 Shunhua Rd, Jinan
2F, Bldg F, University Science Park
Tel: 0531-88819269
Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.
Business Email
E-mail: product@genelibs.com