| Autor: |
Matsuka, Yury V., Migliorini, Mary M., Ingham, Kenneth C. |
| Zdroj: |
Journal of Protein Chemistry; November 1997, Vol. 16 Issue: 8 p739-745, 7p |
| Abstrakt: |
Fibronectin binds specifically to fibrin and is covalently cross-linked to the fibrin α chain by activated factor XIII (XIIIa). This reaction is important for wound healing. Here we investigate XIIIa-catalyzed cross-linking of fibronectin and some of its fragments to a recombinant fragment representing the COOH-terminal 30kDa of the fibrin α chain (αC30K:His 368–Val 610). Only fibronectin and those fragments containing an intact NH2-terminus were able to form cross-linked complexes. As many as 10 of the 17 lysines in αC30K can serve as amine donors in this reaction. Analysis of the rate of XIIIa-catalyzed cross-linking of fibronectin NH2-terminal peptides and fragments with αC30K revealed that the presence of the first type I “finger” module accelerates the cross-linking reaction; addition of fingers 2–5 had no further effect. |
| Databáze: |
Supplemental Index |
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