A plasminogen activator from benign ovarian cystadenoma: partial purification and characterization.
A plasminogen activator has been partially purified from benign serous cystadenomas by a combination of Sephadex G-200 gel filtration, CM-Sephadex ion exchange, Concanavalin A-Sepharose and arginine-Sepharose affinity chromatographies. Its apparent size was very large and could not penetrate Sepharose 6B or 5% SDS polyacrylamide gel. It hydrolyzed plasminogen in a manner similar to that of urokinase in terms of their apparent Michaelis constants, although a one-minute lag period had to be allowed for this activation before the hydrolysis of plasminogen. It was very sensitive to reducing agent such that 5 mM dithiothreitol could completely destroy its activity. The activator crossreacted with anti-uterine plasminogen activator IgG, but did not react with anti-urokinase at all. It also bound fibrin well. In the absence of plasminogen, the activator was devoid of amidolytic activity towards S-2251, S-2302 and S-2288 but had a small but measurable activity against S-2444.
D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003537:Cystadenoma / Q000201:enzymology*; D004229:Dithiothreitol / Q000494:pharmacology; D005260:Female; D006801:Humans; D007700:Kinetics; D010051:Ovarian Neoplasms / Q000201:enzymology*; D010958:Plasminogen / Q000378:metabolism; D010960:Plasminogen Activators / Q000276:immunology / Q000302:isolation & purification* / Q000494:pharmacology
D010958:Plasminogen; D010960:Plasminogen Activators; D004229:Dithiothreitol