Hydrolase purified from human plasma
AssigneeCutter Laboratories, Inc.
InventorMichael H. Coan
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Abstract
A previously undescribed hydrolytic enzyme has been successfully isolated from human plasma and purified to homogeneity. The enzyme has a molecular weight of about 70,000 daltons, has a Km for the substrate H-D-Phe-Pip-Arg-PNA of about 0.057 mM, a K.sub.I for benzamidine of about 1.1.times.10.sup.-5 M, is bindable to and elutable from insoluble barium salts, is inhibited by antithrombin III, especially in the presence of heparin, and, in vitro, has been found to activate and degrade human Factor VIII, activate human Factor V, and inhibit platelet aggregation induced by ADP, epinephrine, or collagen, thus providing a substance useful for antithrombotic studies.
Claims3
An enzyme preparation comprising a substantially homogeneous hydrolytic enzyme characterized by being obtainable from human plasma, having a molecular weight of about 70,000 daltons as determined by comparative polyacrylamide gel electrophoresis, having a K.sub.m for the substrate H-D-Phe-Pip-Arg-PNA of about 0.057 mM, having a K.sub.I for benzamidine of about 1.1.times.10.sup.-5 M, being bindable to and elutable from insoluble barium salts, and, in vitro, capable of activating and degrading human Factor VIII, activating human Factor V, and inhibiting platelet aggregation induced by epinephrine, ADP, or collagen.
Dependencies are inferred from the claim text.