Cytochrome b5-like heme/steroid binding domain

By Sephadex gel filtration IS-cytochrome was separated into two hemoprotein components, both having almost the same spectral properties. The large component (molecular weight, ∼120,000) was labile and converted gradually to the small one (molecular weight, ∼12,000) on incubation of mitochondria in the hypotonic medium. Although both components could reconstitute an NADH-cytochrome c reductase system when coupled with microsomal NADH-cytochrome b 5 reductase, their efficiencies in this system were much lower than that of cytochrome b 5 . Neither of the IS-cytochrome components reacted with an antibody to rat liver microsomal cytochrome b 5 .

Cytochrome b5-like heme/steroid binding domain

cytochrome b5-like heme/steroid binding domain

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cytochrome b5-like heme/steroid binding domaincytochrome b5-like heme/steroid binding domaincytochrome b5-like heme/steroid binding domaincytochrome b5-like heme/steroid binding domaincytochrome b5-like heme/steroid binding domain

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