Purification and Characterization of Carboxypeptidase B from Chicken Pancreas

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Carboxypeptidase B was purified by about 74-fold with an overall recovery of 3.3% from chicken pancreas. The enzyme occurs as a monomer and has a molecular weight of about 35, 000 as estimated by polyacrylamide-gel 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 pH7.0-9.5, and was optimal at pH8.5. The Michaelis constant (Km) value for tuppuryl-L-arginine was estimated to be 0.07mM. The isoelectric point of the enzyme was at pH4.6. Although the activity of the enzyme was not inhibited by cobalt chloride, soybean trypsin inhibitor or phenylmethanesulfonyl fluoride, it was inhibited by o-phenanthroline, ethylenediaminetetraacetic acid, 8-hydroxyquinoline and cadmium acetate.
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