May 1, 1993

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

Biomedical Chromatography : BMC
D LinderA Sziegoleit


Human pancreatic carboxypeptidase A, which was isolated from a pool of necrobiotic pancreae, crystallized spontaneously and appeared homogenous 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% homologous in their 31 amino terminal amino acids. On the other hand, amino terminal sequences of the isoenzymes were found to be 79% and 87% homologous with CAP1 and CPA2 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.

  • References11
  • Citations1


Mentioned in this Paper

Crystal - Body Material
Carboxypeptidase A5
Pancreatic Carboxypeptidase A Activity
Amino Acids, I.V. solution additive
TRAF3 gene
Homologous Sequences, Amino Acid
Sequence Analysis
High Pressure Liquid Chromatography Procedure

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