Abstract
Summary
A study was made of the activity of chicken pancreatic enzymes toward synthetic substrates known to be hydrolyzed by bovine trypsin, chymotrypsin, and carboxypeptidase. When activated with bovine trypsin, preparations from chicken pancreas hydrolyzed all of the synthetic substrates tested, and also exhibited proteolytic activity toward denatured hemoglobin. Unactivated preparations exhibited little or no activity toward proteins or synthetic substrates. Trypsin-like and chymotrypsin-like activities were inhibited by diisopropylphosphofluoridate, and by naturally occurring trypsin inhibitors from soybeans, lima beans, and pancreas. The optimum activity for hydrolysis of trypsin substrates was at pH 8.5 to 9.0, and for chymotrypsin substrates was from pH 8.3 to 8.7. The significance of comparative biochemical studies of proteolytic enzymes of different species is discussed.
It is a pleasure to acknowledge the technical assistance of Ruth J. Hurley. We are also indebted to John Bradley, Dept. of Poultry Science, to Magness and Sons Poultry Processing, and to Brazos County Producers Cooperative Assn. for their cooperation in providing the chicken pancreases.
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