Fungal proteases and the mammalian kinin system. II. Kinin hydrolysis by brinolase. |
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Authors: | H J Freedman H J Wilkens N Back |
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Institution: | Department of Biochemical Pharmacology School of Pharmacy State University of New York at Buffalo Buffalo, N.Y. 14207, USA |
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Abstract: | Brinolase, a thrombolytic fungal protease capable of forming vasoactive kinins, has been shown to hydrolyze kinins after their formation. Using synthetic bradykinin as a substrate, the kinetics and mechanism of hydrolysis have been elucidated, evidently explaining the apparently low kinin formation , Bradykinin hydrolysis proceeded rapidly with a pH optimum of 7.0–7.5, and a half-life of 5.1 min, using 250 ng/ml bradykinin and 50 μg/ml brinolase. The Km was 3.2×10?6 M and the Vmax was 4.6 × 10?8 mol/liter/min, using 5 μg/ml brinolase. Two-dimensional paper fractionation of the brinolase-bradykinin digest revealed the presence of free arginine amongst the five peptide fragment spots. |
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