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Kinetics of interaction of ligands with carboxypeptidase A

Journal of Inorganic Biochemistry

Jul 1, 1979

E J Billo

PMID: 112218

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Abstract

Rate constants for the interaction of a number of ligands with the active site zinc ion of carboxypeptidase A have been measured at pH 7.0, 25 degrees, 1.0 M NaCl. Polydentate ligands such as EDTA, NTA or CyDta do not accelerate the rate at which the zinc ion dissociates from the protei...read more

Mentioned in this Paper

Sodium Chloride
Phenanthrolines
Ligands
Metal Antagonists
PH Profile Measurement
Zinc
Carboxypeptidase A Activity
Edetic Acid
Ligands Activity
Carboxypeptidase
Paper Details
References
  • References3
  • Citations9
1

Kinetics of interaction of ligands with carboxypeptidase A

Journal of Inorganic Biochemistry

Jul 1, 1979

E J Billo

PMID: 112218

DOI:

Abstract

Rate constants for the interaction of a number of ligands with the active site zinc ion of carboxypeptidase A have been measured at pH 7.0, 25 degrees, 1.0 M NaCl. Polydentate ligands such as EDTA, NTA or CyDta do not accelerate the rate at which the zinc ion dissociates from the protei...read more

Mentioned in this Paper

Sodium Chloride
Phenanthrolines
Ligands
Metal Antagonists
PH Profile Measurement

Related Papers

Paper Details
References
  • References3
  • Citations9
1

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