Location of the binding site in subcomponent C1q for plasma fibronectin.

K B Reid, J Edmondson
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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.

血浆纤维连接蛋白亚组分C1q结合位点的定位。
先前关于纤维连接蛋白与C1q相互作用的研究得出了明显矛盾的结果,因为据报道,球状头区(由胶原酶消化产生)和胶原样结构域(由有限的胃蛋白酶消化产生)都与纤维连接蛋白结合。在这项研究中,125i标记的纤维连接蛋白与固定在塑料微滴板上的完整C1q或胶原酶或胃蛋白酶消化产物的结合进行了研究。还研究了C1q消化产物对C1q-纤维连接蛋白相互作用的抑制作用。结果证实,球状“头”区制剂和胶原样区制剂都可以与纤维连接蛋白相互作用。由于这些研究中使用的片段与C1q分子共享一段共同的氨基酸序列,因此可以得出结论,纤维连接蛋白在C1q上的结合位点位于由C1q分子的三个链中的每一个链的残基81-97组成的区域。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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