Abstract
The proteinases of extracts of salmon ceca were chromatographed on anionic and cationic cellulose columns by gradient salt elution. Several activities were obtained which were specific for the hydrolysis of toluenesulfonyl- l-arginine methyl ester (TAME) or acetyl- l-tyrosine ethyl ester. Considering the elution patterns, electrophoretic properties, and effect of soybean trypsin inhibitor, it appeared that the salmon enzymes in most cases had a physicochemical as well as a functional relationship to mammalian trypsins and chymotrypsins. However, there were generally minor differences and in the most exceptional case pronounced Chromatographic and electrophoretic differences from any known mammalian TAME-hydrolyzing endopeptidase.
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