Demonstration that spleen green hemeprotein is identical to granulocyte myeloperoxidase.
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.
Ikeda-Saito
M
M
Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia 19104-6089.
Lee
H C
HC
Adachi
K
K
Eck
H S
HS
Prince
R C
RC
Booth
K S
KS
Caughey
W S
WS
Kimura
S
S
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002417:Cattle; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004578:Electron Spin Resonance Spectroscopy; D004591:Electrophoresis, Polyacrylamide Gel; D006098:Granulocytes / Q000201:enzymology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000378:metabolism; D013053:Spectrophotometry; D013154:Spleen / Q000201:enzymology*
D009195:Peroxidase