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J. Biochem, 1977, Vol. 81, No. 5 1285-1291
© 1977 Japanese Biochemical Society

research-article

Purification of Carboxypeptidase A Using Sepharose 4B-Bound 3-Phenylpropionate

Genichiro OSHIMA and Kinzo NAGASAWA

School of Pharmaceutical Sciences, Kitasato University Minato-ku, Tokyo 108

The activity of carboxypeptidase A [EC 3.4.12.2 [EC] ] was inhibited by 3-phenylpropionate derivatives (p-aminocinnamate, 3-p-aminophenylpropionate and 3-p-acetylaminophenylpropionate), and to investigate its use as a ligand for affinity chromatography 3-p-aminophenylpropionate was directly and indirectly coupled to Sepharose 4B. Carboxypeptidase A was adsorbed only on 3-p-aminophenylpropionate bound to the gel through p-phenylenediamine as a spacer.

Carboxypeptidase A from pancreas was purified by a combination of this affinity adsorbent and ion exchange chromatography. The purified carboxypeptidase A had a homogeneity similar to that of a commercial product, as judged by disc gel electrophoresis.

The carboxypeptidase activity of Pronase was slightly retarded on the gel column, but could not be separated from its caseinolytic activity. Angiotensin I-converting enzyme [peptidyl dipeptide hydrolase, EC 3.4.15. 1] obtained from hog kidney cortex was not bound to the gel.


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