[Features of the interaction of Glu- and Lys-forms of plasminogen with native and partially hydrolyzed fibrin].
Glu- and Lys-plasminogen interaction with native and desAABB-fibrin obtained from fibrinogen partially hydrolyzed by plasmin was studied. It was found that native fibrin adsorbs 6 times more Lys-plasminogen as compared to the native form of the proenzyme. The range of the Lys-plasminogen binding does not change, if part of the fibrinogen molecules hydrolyze down to X-fragments. At the same time, the appearance in the system of 1% Xi-fragments leads to a 6-fold increase in the Glu-plasminogen binding. The amount of adsorbed Glu-plasminogen reaches the level of Lys-plasminogen adsorption both in the native and partially hydrolyzed fibrin. It was found that kringle K 1-3 or 6-aminohexanoic acid at saturating for high-affinity lysine-binding sites concentrations do not influence the Glu-plasminogen binding to native fibrin but inhibit it when the partially purified form is used. It is assumed that the manyfold increase of the Glu-plasminogen binding to partially hydrolyzed fibrin is due to the alteration of the proenzyme conformation at the initial steps of fibrin hydrolysis during the formation of Xi fragments.
Grinenko
T V
TV
Skomorovskaia
E V
EV
Kudinov
S A
SA
Zolotareva
E N
EN
D015119:Aminocaproic Acid / Q000494:pharmacology; D001120:Arginine / Q000494:pharmacology; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005337:Fibrin / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D010958:Plasminogen / Q000302:isolation & purification / Q000378:metabolism*
D010446:Peptide Fragments; C018998:lysyl-plasminogen; D005337:Fibrin; D005340:Fibrinogen; D010958:Plasminogen; D001120:Arginine; D015119:Aminocaproic Acid
Osobennosti vzaimodeĭstviia Glu- i Lys-form plazminogena s nativnym i chastichno gidrolizovannym fibrinom.