The isolation and characterization of a new form of porcine pancreatic carboxypeptidase A (carboxypeptidase Ae)

Abstract
A new porcine carboxypeptidase A, designated as Ae, has been isolated from twice crystallized elastase. The enzyme preparation appeared homogeneous in the ultracentrifuge and gel electrophoresis, and had an s20,w of 3.34 S. A molecular weight of 34 700 was obtained from sedimentation equilibrium and the zinc content was 0.93 mole/mole enzyme. The new enzyme differs from the known porcine carboxy-peptidases (Aj, A2, A3) in solubility properties and amino acid composition. The amino acid compositions of Ai, A2, and Ae, which mainly differ in the content of isoleucine, are suggestive of their being genetic variants due to several amino acid replacements in the molecule.

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