Abstract
Bothrops protease A, one of the proteolytic enzymes found in the venom of the snake, Bothrops jararaca, was purified by a method which leads to the same purification but gives a better yield than the method previously used. The hydrolytic potency of Bothrops protease A on p-toluenesulfonyl- l-arginine methyl ester, benzoyl- l-arginine amide, protamine, and l-lysine ethyl ester was found to be one half, one eighth, one ninth, and one hundredth as great as that of crystalline trypsin, respectively. Bothrops protease A was found to be stable at room temperature between pH 3 and 9.
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