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LAWRENCE O. ELY, M.D.

AMA Arch Ophthalmol. 1952;47(6):717-719.

	Since this article does not have an abstract, we have provided the first 150 words of the full text PDF and any section headings.

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.

METHODS

A quantitative spectrophotometric determination was made to see whether cytochrome c . . . [Full Text PDF of this Article]

Author Affiliations
IOWA CITY

From the Departments of Surgery, Physiology, and Ophthalmology, University Hospitals.

Footnotes
Supported in part by a grant from the John and Mary R. Markle Foundation.

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