Abstract
A purified hepatic microsomal mixed-function drug oxidase (EC 1.14.13.8) catalyzes oxidation of cysteamine to cystamine. Since cysteamine is a normal intracellular metabolite, this reaction could provide an enzymic mechanism for the continuous generation of disulfides required for formation of disulfide bonds in newly synthesized proteins. This hypothesis was tested by studying the renaturation of reduced ribonuclease in media containing glutathione reductase, purified microsomal oxidase, an NADPH-generating system, and physiological concentrations of glutathione and cysteamine. Under these conditions renaturation of reduced-disorganized ribonuclease is completely dependent upon the microsomal oxidase, and optimal renaturation rates are obtained when the relative activities of glutathione reductase and cysteamine oxidase approximate levels present in whole liver homogenates.
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