THE CRYSTALLINE lens is rich in both pyruvic acid1 and its reduction product, lactic acid.2 The citric-acid cycle has been identified as probably playing a role in the utilization of these substrates.3 The 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.4 This 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.4 The present report details another attempt to isolate and to identify cytochrome c in the crystalline lens.
A quantitative spectrophotometric determination was made to see whether cytochrome c
ELY LO. THE CYTOCHROME-C CONTENT OF BOVINE CRYSTALLINE LENS. AMA Arch Ophthalmol. 1952;47(6):717–719. doi:10.1001/archopht.1952.01700030736002
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