Identification of a site in fibrin(ogen) which is involved in the acceleration of plasminogen activation by tissue-type plasminogen activator.

摘要: Abstract The rate of activation plasminogen by tissue-type activator is greatly increased fibrin, but not fibrinogen. A possible explanation for this phenomenon could be that conformational changes take place during the transformation fibrinogen to fibrin which lead exposure sites involved in accelerated plasmin formation. This also supported our recent observation some enzymatically prepared fragments and (D EGTA, D-dimer, Y) CNBr fragment 2 from have property. consists amino acid residues Aα (148–207), Bβ (191–224) + (225–242) (243–305) γ 95–265, kept together disulphide bonds. In order study localization a stimulating site within structure we purified chain remanants after reduction carboxymethylation, found only 148–207 was stimulating. further confirmed digesting pure Aα-chains cwith purifying resulting Aα-chain fragments. digests Bβ- γ-chains were stimulatory. remnant (residue 111–197) D EGTA D-dimer comprise major part (residues 148–197) fragment. We conclude capable accelerating prexists fibrinogen, becomes exposed upon formation or disruption stretch 184–197, retained remnants degradation products.