Cytochrome b-245 from neutrophil plasma membranes contains two types of subunit with apparent molecular masses from gel electrophoresis in the presence of SDS of 23 kDa and 76-92 kDa. Radiation-inactivation analysis revealed a single-exponential decay process for the visible absorption of the haem chromophore in the membrane, corresponding to a molecular mass of 21 +/- 5 kDa for the haem-containing polypeptide chain. Sedimentation equilibrium of the cytochrome solubilized by the detergent Triton N101 showed that the protein was polydisperse, with a molecular mass of approx. 350 kDa for the smallest detectable species. In another detergent, n-octyl beta-O-glucopyranoside (octyl glucoside), the molecular mass of the haem-containing particle was found to be 20-30 kDa. Thus the quaternary structure of the protein breaks down in this detergent. The haem group is inferred to be attached to the smaller subunit.
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December 1989
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Research Article|
December 15 1989
Identification of the haem-binding subunit of cytochrome b−245
J H A Nugent;
J H A Nugent
*Department of Biology, University College London, Gower Street, London WC1E 6JJ
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W Gratzer;
W Gratzer
†M.R.C. Cell Biophysics Unit, Kings College, Drury Lane, London WC2B 5LR, U.K.
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A W Segal
A W Segal
‡Department of Medicine, University College London, Gower Street, London WC1E 6JJ
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1989 London: The Biochemical Society
1989
Biochem J (1989) 264 (3): 921–924.
Citation
J H A Nugent, W Gratzer, A W Segal; Identification of the haem-binding subunit of cytochrome b−245. Biochem J 15 December 1989; 264 (3): 921–924. doi: https://doi.org/10.1042/bj2640921
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