[Mechanism of retardation of fibrin polymerization using a thermostable inhibitor from human serum].
A purified thermostable inhibitor of fibrin polymerization was found to have a molecular mass of 1,750 +/- 100 daltons. Early steps of the fibrin polymerization were the most sensitive to the effect of this inhibitor; less distinct but constant activity was exhibited by the inhibitor at later steps of the process. As shown by kinetics of inhibition the inhibitor reacted with fibrin-monomer as well as with more complex products of polymerization but the final products (unstabilized fibrin) did not contain this substance. The inhibitor was found in a number of tissues. The inhibitor appears to be responsible for long-term existence of fibrin-monomer in circulation.
D005337:Fibrin / Q000037:antagonists & inhibitors* / Q000502:physiology; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight
D046911:Macromolecular Substances; D005337:Fibrin
K Mekhanizmu tormozheniia samosborki fibrina termostabli'nym ingibitorom syvorotki krovi.