Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 13 January 1961:
Vol. 133. no. 3446, pp. 100 - 101
DOI: 10.1126/science.133.3446.100
Prev | Table of Contents | Next

Articles

Cytochrome c Reductase of Tri- and Diphosphopyridine Nucleotides in Rat Lens

Sidney Lerman 1

1 Department of Surgery, University of Rochester School of Medicine and Dentistry, Rochester, New York

The ocular lens of the 28- to 32-day-old rat contains an active hexose monophosphate shunt pathway for the combustion of glucose. Triphosphopyridine nucleotide (TPNH) cytochrome c reductase is present in this organ and is approximately one-third more active than diphosphopyridine nucleotide (DPNH) cytochrome c reductase. Since there is no transhydrogenase activity in these lenses, and since DPNH lactic dehydrogenase is 15 times as active as TPNH lactic dehydrogenase, the presence of an active TPNH cytochrome c reductase may provide this organ with the means of reoxidizing the relatively large amounts of TPNH formed by the direct oxidative pathway of glucose metabolism. Although TPNH oxidation in other tissues has not as yet been shown to yield adenosine triphosphate (ATP) directly, it is possible that such a mechanism may be operative in the rat lens.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Pathogenetic Factors in Experimental Galactose Cataract: Part IV.
S. LERMAN (1961)
Arch Ophthalmol 65, 334-337
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)