[Interaction of a peptide inhibitor with two forms of monomeric fibrin differing in the degree of activation].
The study is devoted to the interaction of peptide inhibitor of fibrin self-assemblage with two forms of fibrin monomer: deprived of fibrinopeptides A and preserving fibrinopeptides B (desAA-monomer) and fully activated (desAABB-monomer). It is shown that peptide inhibitor hinders the coagulative conversion of fibrinogen by thrombin, limiting the enzymic and nonenzymic stages of the process. The indispensible condition for the formation of inhibitor-monomeric fibrin associates is a preliminary modification of fibrinogen by thrombin.
Chiriat'ev
E A
EA
Leonova
O P
OP
Byshevskiĭ
A Sh
ASh
D000818:Animals; D002417:Cattle; D005337:Fibrin / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D005344:Fibrinopeptide A / Q000378:metabolism*; D005345:Fibrinopeptide B / Q000378:metabolism*; D010455:Peptides / Q000037:antagonists & inhibitors*; D013917:Thrombin / Q000378:metabolism
D010455:Peptides; D005344:Fibrinopeptide A; D005345:Fibrinopeptide B; D005337:Fibrin; D005340:Fibrinogen; D013917:Thrombin
Vzaimodeĭstvie peptidnogo ingibitora s dvumia formami monomernogo fibrina, razlichaiushchimisia po stepeni aktivatsii.