[Prothrombin activation by immobilized thrombin].
The ability of thrombin, immobilized on BrCN-activated Sepharose 4B, to split prothrombin, was studied. Immobilized thrombin retained up to 70% of its esterase activity and about 5% of its coagulating activity; it was also found to induce partial proteolysis of prothrombin. Two products of prothrombin degradation isolated, i.e. P1 (m. w. 50.000-52.000) and P2 (m. w. 22.000-24.000), did not show either the thrombin or the prothrombin activities. P1 was converted into thrombin under the action of tripsin or Factor Xa. The rate of conversion was considerably increased after addition of Factor V, thromboplastin and Ca2+ ions. Intravenous administration of P1 to rats resulted in changes in the coagulating system of blood, which may be probably indicative of the stimulation of the anticoagulating system. P2 possessed no thrombogenic activity.
D000818:Animals; D001777:Blood Coagulation / Q000187:drug effects; D004789:Enzyme Activation; D004800:Enzymes, Immobilized; D005170:Factor X; D010446:Peptide Fragments / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000378:metabolism; D011516:Prothrombin / Q000378:metabolism*; D051381:Rats; D012685:Sepharose; D013917:Thrombin / Q000378:metabolism*; D014357:Trypsin
D004800:Enzymes, Immobilized; D010446:Peptide Fragments; D011516:Prothrombin; D005170:Factor X; D012685:Sepharose; D010447:Peptide Hydrolases; D014357:Trypsin; D013917:Thrombin
Aktivatsiia protrombina immobilizovannym trombinom