Abstract
A new, practical, and quantitative method for the determination of tryptic enzyme activity is reported. The method is based on measurements of the U.V. absorption of the complex formed between cupric ion and Nα-p-toluenesulphonyl-L-arginine, the latter being the product of the reaction between the tryptic enzymes (thrombin, trypsin, plasmin) and the corresponding methyl ester. Comparisons with the null point titration procedure demonstrate the new method's superiority when dealing with enzyme–substrate reactions in concentrated buffer solutions. Under certain conditions, it could also be superior in dilute buffer situations. The effects of pH and cupric ion concentration on complex formation are discussed along with other characteristics of the U.V. absorption curves of the complex.
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