title: [Fibrinolytic action of an enzyme preparation covalently bound to modified thrombin].
abstract: Successive thrombin modification by carbodiimide and aliphatic diamines decreases esterase and fibrin-coagulating activity of the enzyme. Modified thrombin causes no platelet aggregation. Water-soluble enzyme conjugates devoid of fibrinogen-coagulating action and possessing increased fibrinolytic affinity to the site of fibrin clot location have been obtained by covalent binding of chymotrypsin to modified thrombin.
mesh_terms: D000345:Affinity Labels / Q000378:metabolism; D002918:Chymotrypsin / Q000378:metabolism / Q000494:pharmacology*; D003959:Diamines / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D005022:Ethyldimethylaminopropyl Carbodiimide / Q000031:analogs & derivatives / Q000494:pharmacology; D005342:Fibrinolysis / Q000187:drug effects*; D066298:In Vitro Techniques; D008722:Methods; D010974:Platelet Aggregation / Q000187:drug effects; D013329:Structure-Activity Relationship; D013917:Thrombin / Q000378:metabolism / Q000494:pharmacology*
chemical_list: D000345:Affinity Labels; D003959:Diamines; C041829:1-ethyl-3-(3-(dimethylamino)propyl)carbodiimide methiodide; D002918:Chymotrypsin; D013917:Thrombin; D005022:Ethyldimethylaminopropyl Carbodiimide
vernacular_title: Fibrinoliticheskoe deĭstvie fermentnogo preparata, kovalentno sviazannogo s modifitsirovannym trombinom.