Abstract
THE CRYSTALLINE lens is rich in both pyruvic acid1and its reduction product, lactic acid.2The citric-acid cycle has been identified as probably playing a role in the utilization of these substrates.3The final hydrogen mediator in the lens is unknown. Previous experiments indicate that a large portion of the respiration of the crystalline lens is inhibited by cyanide.4This fact indicates that the normal oxygen consumption of bovine crystalline lens is dependent on the presence of a heavy metal-containing enzyme, most probably iron. The commonest enzyme system which is dependent on the presence of iron is the cytochromecytochrome oxidase system. A previous attempt to isolate and identify cytochrome c in the lens met with failure.4The present report details another attempt to isolate and to identify cytochrome c in the crystalline lens. METHODS A quantitative spectrophotometric determination was made to see whether cytochrome c
Published Version
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