Reagents for reversible coupling of proteins to the active centres of trypsin-like serine proteinases.
In order to extend the scope for the application of acyl-enzymes as fibrinolytic agents, p-amidinophenyl ester enzyme substrates were prepared that gave stabilized acyl-enzymes capable of being coupled to other proteins. Coupling was achieved by reaction of protein thiol functions with a 2-pyridyldithio moiety within the acyl group. Acyl-enzymes derived from such substrates were stable enough to permit isolation of reversible conjugates between proteins and the active centres of plasminogen activators. Hydrolytic release of active enzyme from a conjugate of human immunoglobulin G and urokinase could be demonstrated.
D000578:Amidines / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D002850:Chromatography, Gel; D004220:Disulfides / Q000378:metabolism; D005341:Fibrinolysin / Q000378:metabolism; D006868:Hydrolysis; D007074:Immunoglobulin G / Q000276:immunology; D046911:Macromolecular Substances; D011725:Pyridines / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000378:metabolism*; D014568:Urokinase-Type Plasminogen Activator / Q000276:immunology / Q000378:metabolism
D000578:Amidines; D002352:Carrier Proteins; D004220:Disulfides; D007074:Immunoglobulin G; D046911:Macromolecular Substances; D011725:Pyridines; D012697:Serine Endopeptidases; D005341:Fibrinolysin; D014568:Urokinase-Type Plasminogen Activator