[Lysine- and arginyl-binding sites of plasminogen domains].

Hydrolysis of plasminogen permits obtaining its nine fragments. The method of differential scanning microcalorimetry reveals seven domains in plasminogen, and the affinity chromatography--three lysin- and three arginyl-binding sites. The lysin-binding sites of domains (Kringles) K1 and K4 differ in ligand specificity. Benzamidine-binding sites of domain K5 and of plasmin light chain are simultaneously arginine-binding ones. The third arginyl-binding site differing from the benzamidine-binding one is found in fragment K1-3. In the plasminogen-fibrin interaction only lysin-binding sites of plasminogen take part; in the plasminogen fragments-fibrinogen fragments interaction both types of plasminogen sites participate. The heavy chain of plasmin interacts with the E-fragment of fibrinogen by the lysin-binding sites, and the light chain of plasmin interacts with D-fragment of fibrinogen by arginyl-binding sites. Sites complementary to arginyl binding sites of plasminogen are located on the DH-fragment and sites of interaction with lysin- and arginyl-binding sites--on the DL-fragment. The plasmin-fibrin interaction mediated by sites of the first four cringles is not associated with changes in the catalytic function of the active centre. Interaction of Lys-plasminogen with fibrin accelerates polymerization of the latter. The effect of Lys-plasminogen is conditioned by the lysin-binding sites. Glu-plasminogen has no effect on the polymerization process.