Identification and characterization of eight porcine pancreatic proteinases, carboxypeptidase A and amylase after electrophoretic separation using specific substrates.
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: Anodal and cathodal trypsin with Bz-Arg-pNA. 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-beta NE and with differences in their molecular weights and electrophoretical charges. Elastase I and protease E with Suc-(Ala)3-pNA and MeO-Suc-Ala-Ala-Pro-Val-pNA and elastase I also with elastin. Elastase II with the chymotrypsin substrates and with elastin. Carboxypeptidase A with CN-Phe. Amylase with blue starch polymer.
D000595:Amino Acid Sequence; D000681:Amylases / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D002268:Carboxypeptidases / Q000302:isolation & purification* / Q000378:metabolism; D043422:Carboxypeptidases A; D004587:Electrophoresis, Agar Gel / Q000379:methods; D010179:Pancreas / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity; D013552:Swine
D000681:Amylases; D002268:Carboxypeptidases; D010447:Peptide Hydrolases; D043422:Carboxypeptidases A