Abstract
Cytochrome b, and NADH-dependent cytochrome 6,reductase (EC 1.6.2.2) are components of electron transport systems. In the endoplasmic reticulum of liver and many other tissues the proteins are involved in the desaturation of fatty acids (Oshino & Sato, 1971) and in the cytochrome I-’150-mediated metabolism of endogenous compounds such as steroids, and of foreign compounds including many drugs, carcinogens and environmental pollutants (Ortiz de Montellano, 1986). In the cytosol of mature erythrocytes, cytochrome b, and cytochrome-b, reductase are present as smaller water-soluble species that are responsible for the reduction of methaemoglobin (Hultquist & Passon, 197 1). The inherited disorder methaemoglobinaemia can be due to a homozygous deficiency of erythrocyte cytochrome-b, reductase (Scott & Griffith, 1959; Hultquist & Passon, 1971) or, in at least one case, to a deficiency of cytochrome b, (Hegesh et al., 1986). In this paper we report the isolation and characterization of rat and human cDNA and rat genomic DNA clones coding for cytochrome b,, and a human cDNA clone coding for cytochrome h,-reductase.
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