[Role of the K4 and K5 plasmin heavy chain kringles in the fibrin clot structure destruction].
A comparative analysis of the rates of polymeric fibrin structure destruction by plasmin (Pm) and its proteolytic derivatives such as Val354-plasmin (c-Pm), Val442-plasmin (m-Pm) and Lys530-plasmin (mu-Pm) has been undertaken. It was shown, that Pm, c-Pm, m-Pm and mu-Pm at equal proteolytic activity, have dissolved fibrin clots with relative rates 40.3:38.0:4.6:1.0 correspondingly. The Pm, m-Pm and mu-Pm relative rates were changed by epsilon-aminocaproic acid to 4.6:1.5:1.0 correspondingly. In this case fibrin clot destruction time was increased for Pm and m-Pm and was not changed for mu-Pm. The rates of fibrinogen hydrolysis were nearly equal for these forms of enzyme. It was suggested, that the specific interactions between plasmin K4 and K5 kringles and solid phase fibrin substrate determine the polymer fibrin structure destruction rate.
Andrianov
S I
SI
Makogonenko
E M
EM
Kudinov
S A
SA
D015119:Aminocaproic Acid / Q000494:pharmacology; D001704:Biopolymers; D005337:Fibrin / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism; D005341:Fibrinolysin / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D013927:Thrombosis / Q000378:metabolism*
D001704:Biopolymers; D005337:Fibrin; D005340:Fibrinogen; D005341:Fibrinolysin; D015119:Aminocaproic Acid
Rol' kringlov K4 i K5 tiazheloĭ tsepi plazmina v razrushenii struktury fibrinovogo sgustka.