Separation of human pancreatic carboxypeptidase A isoenzymes by high performance liquid chromatography

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Abstract
Human pancreatic carboxypeptidase A, which was isolated from a pool of necrobiotic pancreae, crystallized spontaneously and appeared homogeneous in sodium dodecylsulphate polyacrylamide gel electrophoresis. Reversed phase high performance liquid chromatography of the dissolved crystals, however, revealed the presence of two distinct isoenzymes, which were shown by aminoterminal sequence analysis to be only 61% homologeous in their 31 amino terminal amino acids. On the other hand, amino terminal sequences of the isoenzymes were found to be 79% and 87% homologeous with CAP 1 and CPA 2 of the rat, respectively. Thus, the presence of two distinct pancreatic carboxypeptidase A isoenzymes could be clearly demonstrated for the first time in human tissue.