Journal of Biological Chemistry · 1989 · 23 citations · 31 references
Life SciencesBiochemistryMolecular BiologyEnzymologyProtein BiochemistryRedox BiochemistryEnzyme CharacterizationHeme MetabolismHeme Redox ChemistryProtein OxidationRedox EnzymesRedox MetabolismHeme EnzymesHeme Protein Redox PotentialHeme Protein SpectroelectrochemistryHeme Redox Enzyme MechanismsOxidation - Reduction PotentialOxidation-reduction PotentialRedox PropertiesSteady-state Kinetics
The biochemical, spectroscopic, enzymatic, and redox properties of spleen myeloperoxidase, a peroxidase formerly called "spleen green hemeprotein," and granulocyte myeloperoxidase were compared by electrophoresis, amino-terminal amino acid sequences, optical and EPR spectroscopy, steady-state enzyme kinetics, and oxidation-reduction potential. The spleen enzyme exhibits properties indistinguishable from those of the granulocyte enzyme. We conclude that the spleen enzyme is indeed identical to granulocyte myeloperoxidase.
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