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Inhibition of cobalt(II) carboxypeptidase A by ligands. Kinetic evidence for the formation of a ternary enzyme-metal-ligand complex

Journal of Inorganic Biochemistry

Jul 1, 1980

Robert David Rogers, E J Billo

PMID: 7190999

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Abstract

Saturation kinetics are observed in the inhibition of cobalt carboxypeptidase A by the chelating agent 1,10-phenanthroline. The association constant K1 for the formation of the enzyme-metal-ligand ternary complex and k2, the rate of breakup of the ternary complex, have been obtained. A ...read more

Mentioned in this Paper

Ligands
Mathematics
Metazoa
Metabolic Inhibition
PH Profile Measurement
Carboxypeptidase A5
Hydrogen-Ion Concentration
Carboxypeptidase A Activity
Cobalt
Chelating Agents
Paper Details
References

Inhibition of cobalt(II) carboxypeptidase A by ligands. Kinetic evidence for the formation of a ternary enzyme-metal-ligand complex

Journal of Inorganic Biochemistry

Jul 1, 1980

Robert David Rogers, E J Billo

PMID: 7190999

DOI:

Abstract

Saturation kinetics are observed in the inhibition of cobalt carboxypeptidase A by the chelating agent 1,10-phenanthroline. The association constant K1 for the formation of the enzyme-metal-ligand ternary complex and k2, the rate of breakup of the ternary complex, have been obtained. A ...read more

Mentioned in this Paper

Ligands
Mathematics
Metazoa
Metabolic Inhibition
PH Profile Measurement

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