The Specificity of Trypsm by Max Bergmann,
نویسنده
چکیده
The isolation of two proteinases in crystalline form from extracts of beef pancreas has been described by Kunitz and Northrop (1). These enzymes have been named trypsin and chymotrypsin. Previous publications (2) from this laboratory have reported the finding of a series of synthetic peptide derivatives which were readily hydrolyzed by crystalline chymotrypsin. In this communication a synthetic substrate for crystalline trypsin is described. or-Benzoyl-Larginineamide hydrochloride (I) is hydrolyzed extremely rapidly by crystalline trypsin (recrystallized three times) to yield benzoyl-Z-arginine and ammonia (cf. Table I). This hydrolysis proceeds optimally at about pH 7.8 (Fig. 1).
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The Activation of Papain Trypsinase as a Function of the Nature of the Activator by George W. Irving, Jr., Joseph S. Fruton, and Max Bergmann
Papain contains a cysteine-activatable proteinase that hydrolyzes benzoyll-arginlneamide (1). This enzyme has been shown to have a specificity similar to that of crystalline pancreatic trypsin (2) and therefore has been designated papain trypsinase (3). Previous experiments have shown that papain trypsinase exists in two inactive forms which can be designated papain-a-trypsinase and papain-13-t...
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