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Purification and crystallization of human carboxypeptidase A

Biochemistry

Jun 15, 1976

Leif PetersonBert L Vallee

PMID: 938622

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Abstract

Human carboxypeptidase A has been isolated from activated pancreatic juice by means of affinity chromatography employing the competitive inhibitor benzylsuccinic acid as an affinity ligand. The structural and functional features of the human and bovine enzymes are quite analogous. The m...read more

Mentioned in this Paper

Enzymes, antithrombotic
Amino Acid [EPC]
Proteolytic Enzyme
Enzymes, peripheral vasodilators
Pancreatic Juice
Benign Melanocytic Nevus
Ligands
Scanning Electron Microscopy
Cadmium Measurement
Alloenzymes
Paper Details
References
  • References27
  • Citations30
123
  • References27
  • Citations30
123

Purification and crystallization of human carboxypeptidase A

Biochemistry

Jun 15, 1976

Leif PetersonBert L Vallee

PMID: 938622

DOI:

Abstract

Human carboxypeptidase A has been isolated from activated pancreatic juice by means of affinity chromatography employing the competitive inhibitor benzylsuccinic acid as an affinity ligand. The structural and functional features of the human and bovine enzymes are quite analogous. The m...read more

Mentioned in this Paper

Enzymes, antithrombotic
Amino Acid [EPC]
Proteolytic Enzyme
Enzymes, peripheral vasodilators
Pancreatic Juice

Related Papers

Paper Details
References
  • References27
  • Citations30
123
  • References27
  • Citations30
123

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