CROSS-LINKING OF FIBRONECTIN TO C-TERMINAL FRAGMENTS OF THE FIBRINOGEN ALPHA -CHAIN BY FACTOR XIIIA
作者： Yury V. Matsuka , Mary M. Migliorini , Kenneth C. Ingham
关键词: Fibrin 、 Bioorganic chemistry 、 Recombinant DNA 、 Covalent bond 、 Wound healing 、 Molecular biology 、 Factor XIIIa 、 Fibrinogen alpha chain 、 Chemistry 、 Fibronectin
摘要: Fibronectin binds specifically to fibrin and is covalently cross-linked the α chain by activated factor XIII (XIIIa). This reaction important for wound healing. Here we investigate XIIIa-catalyzed cross-linking of fibronectin some its fragments a recombinant fragment representing COOH-terminal 30kDa (αC30K:His 368–Val 610). Only those containing an intact NH2-terminus were able form complexes. As many as 10 17 lysines in αC30K can serve amine donors this reaction. Analysis rate NH2-terminal peptides with revealed that presence first type I “finger” module accelerates reaction; addition fingers 2–5 had no further effect.
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