CO-reacting haemoproteins of neutrophils: Evidence for cytochrome b-245 and myeloperoxidase as potential oxidases during the respiratory burst

Edwards, Steven W and Lloyd, David ORCID: https://orcid.org/0000-0002-5656-0571 1987. CO-reacting haemoproteins of neutrophils: Evidence for cytochrome b-245 and myeloperoxidase as potential oxidases during the respiratory burst. Bioscience Reports 7 (3) , 193--199. 10.1007/BF01124789

Full text not available from this repository.

Abstract

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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Schools > Biosciences
Publisher:	Portland Press: Creative Commons Attribution / Springer Verlag (Germany)
ISSN:	0144-8463
Last Modified:	26 Oct 2022 08:33
URI:	https://orca.cardiff.ac.uk/id/eprint/127784

Citation Data

Cited 4 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item