[The role of complementary E2 and D2 centers in the reaction between fibrin and fibrinogen].
The effect of fibrinogen on the two steps of polymerization of two fibrin forms differing in the set of polymerization sites (fibrin-desAA and fibrin-desAABB) was studied. It was shown that fibrinogen inhibited the protofibril growth and fibril formation at the stage of lateral aggregation more effectively with fibrin-desAABB than with fibrin desAA. When the fibrinogen D2-site was blocked by tetrapeptide Gly-His-Arg-Pro, the key structure of the E2-site, the inhibitory activity of fibrinogen diminished. A conclusion is drawn that the high susceptibility of fibrin-desAABB to fibrinogen is due to the interaction of the E2-active site with the D2-site of the fibrinogen molecule. The concentration dependence of the tetrapeptide Gly-His-Arg-Pro-induced inactivation of fibrinogen and the effects of temperature and Ca2+ on the tetrapeptide interaction with fibrinogen were investigated.
D005337:Fibrin; D005338:Fibrin Fibrinogen Degradation Products; D005340:Fibrinogen; D006801:Humans; D009842:Oligopeptides; D011108:Polymers
D005338:Fibrin Fibrinogen Degradation Products; D009842:Oligopeptides; D011108:Polymers; C046678:fibrinopeptide D; C046679:fibrinopeptide E; C048770:glycyl-histidyl-arginyl-proline; D005337:Fibrin; D005340:Fibrinogen
Rol' komplementarnykh tsentrov E2 i D2 v reaktsii mezhdu fibrinom i fibrinogenom.