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. 1995:255:476-87.
doi: 10.1016/s0076-6879(95)55050-x.

Purification of human neutrophil NADPH oxidase cytochrome b-558 and association with Rap 1A

M T Quinn  1 , C A Parkos, A J Jesaitis
Affiliations

Purification of human neutrophil NADPH oxidase cytochrome b-558 and association with Rap 1A

M T Quinn et al. Methods Enzymol. 1995.

Abstract

The availability of sufficient quantities of highly purified phagocyte cytochrome b-558 has been necessary for many of the biochemical and immunological analyses of this important NADPH oxidase component, and it was only through the analysis of highly purified cytochrome b that the subunit composition was elucidated and the small subunit (p22-phox) was cloned and sequenced. In addition, the association of the small GTP-binding protein Rap1A with cytochrome b-558 was discovered through the analysis of purified cytochrome b. The procedures described here provide an easy, efficient, and highly reproducible method for the purification of cytochrome b as well as cytochrome b-Rap1A complexes. The ability to purify cytochrome b and cytochrome b-Rap1A complexes will also allow further analysis of the structure of this novel plasma membrane redox protein and the role of its association with low molecular weight GTP-binding proteins in the structure and regulation of the phagocyte NADPH oxidase.

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