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

Biomedical Chromatography : BMC

Jan 1, 1993

Dietmar LinderA Sziegoleit

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Abstract

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, ...read more

Mentioned in this Paper

CPA1 gene
Homologous Sequences, Amino Acid
Homologous Gene
Crystal - Body Material
CAP1 gene
Pancreatic Carboxypeptidase A Activity
Sequence Analysis
Alloenzymes
Isoenzymes
Human Tissue
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Separation of human pancreatic carboxypeptidase A isoenzymes by high performance liquid chromatography

Biomedical Chromatography : BMC

Jan 1, 1993

Dietmar LinderA Sziegoleit

PMID: 8318831

DOI: 10.1002/bmc.1130070308

Abstract

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, ...read more

Mentioned in this Paper

CPA1 gene
Homologous Sequences, Amino Acid
Homologous Gene
Crystal - Body Material
CAP1 gene

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Paper Details
References
  • References11
  • Citations
12
  • References11
  • Citations
  • quote and clock

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    This paper may not have been cited yet.

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