| Autor: |
Medved LV; Institute of Biochemistry, Academy of Sciences of Ukraine, Kiev., Litvinovich SV, Ugarova TP, Lukinova NI, Kalikhevich VN, Ardemasova ZA |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 1993 Apr 12; Vol. 320 (3), pp. 239-42. |
| DOI: |
10.1016/0014-5793(93)80594-k |
| Abstrakt: |
Dansyl-labeled tetrapeptide Gly-His-Arg-Pro which mimics the central fibrin polymerization site was used to investigate its binding to a number of fibrinogen fragments containing different numbers of domains. The tetrapeptide was found to bind to fragments DH(95 kDa), DL(82 kDa) and DY(63 kDa) but not to the TSD(28 kDa) fragment. The DY fragment differs from the TSD by the presence of beta and beta C domains. Therefore these domains, which are formed by the C-terminal part of the beta chain, possess a polymerization site complementary to the Gly-His-Arg containing counterpart. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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