CO-reacting haemoproteins of neutrophils: evidence for cytochrome b-245 and myeloperoxidase as potential oxidases during the respiratory burst.
Room temperature, CO-difference spectra of intact rat polymorphonuclear leucocytes (neutrophils) revealed the presence of a number of CO-binding haemoproteins. Absorption maxima at 413, 540 and 570 nm were attributed to the CO-complex of cytochrome b-245 whereas an absorption maximum at 595 nm was assigned to the contribution from a myeloperoxidase complex, since an identical absorption maximum was observed in CO-difference spectra of purified myeloperoxidase in the presence of H2O2. Photochemical action spectra for the relief of CO-inhibited O2 uptake revealed contributions from both cytochrome b-245 and myeloperoxidase. The potential of these two O2- and CO-binding haemoproteins to function as oxidases during the respiratory burst is discussed.
Edwards
S W
SW
Department of Biochemistry, University of Liverpool.
Lloyd
D
D
D000818:Animals; D002248:Carbon Monoxide / Q000032:analysis; D003571:Cytochalasin B / Q000494:pharmacology; D003573:Cytochrome b Group / Q000378:metabolism*; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000494:pharmacology; D009504:Neutrophils / Q000187:drug effects / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism; D009195:Peroxidase / Q000378:metabolism*; D010777:Photochemistry; D051381:Rats; D013053:Spectrophotometry
D003573:Cytochrome b Group; C035130:cytochrome b245; D003571:Cytochalasin B; D009240:N-Formylmethionine Leucyl-Phenylalanine; D002248:Carbon Monoxide; D009195:Peroxidase; D010100:Oxygen