Purification and Characterization of Carboxypeptidase A from Chicken Pancreas

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Carboxypeptidase A was purified by about 59-fold with an overall recovery of 3.5% from chicken pancreas. The enzyme occurs as a monomer and has a molecular weight of about 34, 000 as estimated by polyacrylamidegel electrophoresis (PAGE) and sodium dodecyl sulphate (SDS)-PAGE. The enzyme was stable below 55°C, and the optimal temperature was approximately 45°C. The activity of the enzyme was stable in the range of pH8.0-11.0, and was optimal about pH9. The Michaelis constant (Km) value for hppuryl-L-phenylalanine was estimated to be 0.11mM. The isoelectric point of the enzyme was at pH6.7. Although the activity of the enzyme was not inhibited by soybean trypsin inhibitor or phenylmethanesulfonyl fluoride, it was inhibited by ethylenediaminetetraacetic acid, ophenanthroline, 8-hydroxyquinoline and potato carboxypeptidase inhibitor.
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