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Association of a Ras-related protein with cytochrome b of human neutrophils

ACTIVATION of the superoxide generating system in human neutrophils is thought to involve the interaction or assembly of cytochrome b with other cytosolic and membrane proteins. We have now co-isolated by conventional purification procedures a protein of relative molecular mass 22,000 with cytochrom...

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Bibliographic Details
Published in:Nature (London) 1989-11, Vol.342 (6246), p.198-200
Main Authors: Quinn, Mark T, Parkos, Charles A, Walker, Leslie, Orkin, Stuart H, Dinauer, Mary C, Jesaitis, Algirdas J
Format: Article
Language:English
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Summary:ACTIVATION of the superoxide generating system in human neutrophils is thought to involve the interaction or assembly of cytochrome b with other cytosolic and membrane proteins. We have now co-isolated by conventional purification procedures a protein of relative molecular mass 22,000 with cytochrome b. This Ras-related protein is not a fragment of either of the subunits of cytochrome b , and its primary structure, as determined by the sequencing of its complementary DNA, is identical to that predicted from a recently cloned ras- related gene, rap 1 (also termed Krev-1 ). Immunoaffinity purification on anti-cytochrome and anti-Ras immunoaffinity matrices indicates an association between cytochrome b and the Ras-related protein. The association of a Ras-related GTP-binding protein with cytochrome b of human neutrophils could indicate a role for such a protein in the transduction, regulation or structure of the superoxide generating system.
ISSN:0028-0836
1476-4687
DOI:10.1038/342198a0