Identification of a heparin activated amidolytic enzyme in carp (Cyprinus carpio) plasma.
A heparin activated amidolytic enzyme capable of cleaving synthetic thrombin sensitive chromogenic substrates was identified from the plasma of the carp (Cyprinus carpio). Activation was inhibited by KCl, protamine sulphate and human plasma. Heparin was not required for the continued action of the enzyme. Active enzyme was irreversibly inhibited by DFP. The pH and temperature optima was studied and the enzyme semi purified by Sephadex G100 superfine and Sephadex A50 chromatography. An approximate MW of 62,000 was found. Activity generated by as little as 0.002 units of heparin per ml carp plasma was detected. The trivial name carpamidase is proposed for the enzyme.
D000818:Animals; D002347:Carps / Q000097:blood*; D002850:Chromatography, Gel; D002863:Chromogenic Compounds; D003530:Cyprinidae / Q000097:blood*; D004789:Enzyme Activation / Q000187:drug effects*; D005170:Factor X / Q000032:analysis; D006493:Heparin / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D011516:Prothrombin / Q000032:analysis; D013379:Substrate Specificity; D013696:Temperature
D002863:Chromogenic Compounds; D011516:Prothrombin; D005170:Factor X; D006493:Heparin; D010447:Peptide Hydrolases; C036699:carpamidase