Identification and characterization of eight porcine pancreatic proteinases, car☐ypeptidase A and amylase after electrophoretic separation using specific substrates

Abstract

1. Porcine pancreatic hydrolases in juice and homogenate surveyed by electrophoretic separation in agarose gel, at pH 8.6 and subsequently characterized using substrates of various specificity, either directly in the gel or after transfer to nitrocellulose (enzymoblotting) showed: 2. Anodal and cathodal trypsin with Bz Arg pNA. 3. Chymotrypsin A, B, and C with similar, but not identical, activities to Suc Ala Ala Pro Phe pNA, Bz Tyr pNA, Suc Phe pNA and Ac Phe βNE and with differences in their molecular wieghts and electrophoretical charges. 4. Elastase I and protease E with Suc (Ala) 3 pNA and MeO Suc Ala Ala Pro Val pNA and elastase I also with elastin. 5. Elastase II with the chymotrypsin substrates and with elastin. 6. Car☐ypeptidase A with CN Phe. 7. Amylase with blue starch polymer.