Action of Trypsin Upon Synthetic Poly-ε-Aminocaproyl-α-Alanines*

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Abstract
The synthesis of several linear poly-ε-aminocaproyl-α-amino acids such as poly-ε-aminocaproyl-DL-alanine have recently been achieved by Noguchi and his coworkers with the aid of “theirεN-carbothiophenylamino acid method”(1). Among these synthetic polymers, poly-ε-aminocaproyl-DL-alanine (2), poly-ε-aminocaproyl-α-aminoisobutyric acid (3), and poly-ε-aminocaproyl-L-proline (4), the Benee-Jones protein like substance, possess an unusual property-they are reversibly coagulated by heat in acidic or neutral aqueous solution (2–4). In the previous communication (5) the author briefly reported that these polymers can be partly hydrolysed by the action of trypsin if relatively high concentrations of the enzyme are employed. In the present paper the author wishes to report more extensive studies on this tryptic behavior and the effect of temperature on the enzymatic hydrolysis of poly-ε-aminocaproyl-α-alanines.

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