OSTRICH (STRUTHIO-CAMELUS) CARBOXYPEPTIDASE-A - PURIFICATION, KINETIC-PROPERTIES AND CHARACTERIZATION OF THE PANCREATIC-ENZYME

1. Carboxypeptidase A(beta) and carboxypeptidase A(tau)-type from the pancreas of the ostrich were purified by water extraction of acetone p owder, aminobenzylsuccinic acid affinity and hydroxylapatite chromatog raphy. 2. The final preparations were homogeneous when subjected to SD S-PAGE and PAGE. The M(r) values obtained from SDS-PAGE for CPA(beta) and CPA(tau)-type were 34,600 and 34,400, respectively. 3. The effects of inhibitors (1,10 phenanthroline and indole-3-acetic acid), pH and temperature on CPA activity were examined. K-i-values for CPI, PPA, D- phe, D-trp and aminobenzylsuccinic acid were determined. 4. K-m, k(cat ) and k(cat)/K-m values were determined for hipp-phe, cbz-gly-phe, cbz -(gly)(2)-phe, cbz-gly-leu, cbz-(gly)(2)-leu and cbz-(gly)(2)-val. 5. N-terminal sequencing and amino acid analysis were performed for CPA(b eta) and CPA(tau)-type.