Enzyme/crystallins and extremely high pyridine nucleotide levels in the eye lens.

Published

Journal Article

Taxon-specific crystallins are proteins present in high abundance in the lens of phylogenetically restricted groups of animals. Recently it has been found that these proteins are actually enzymes which the lens has apparently adopted to serve as structural proteins. Most of these proteins have been shown to be identical to, or related to, oxidoreductases. In guinea pig lens, which contains zeta-crystallin, a protein with an NADPH-dependent oxidoreductase activity, the levels of both NADPH and NADP+ are extremely high and correlate with the concentration of zeta-crystallin. We report here nucleotide assays on lenses from vertebrates containing other enzyme/crystallins. In each case where the enzyme/crystallin is a pyridine nucleotide-binding protein the level of that particular nucleotide is extremely high in the lens. The presence of an enzyme/crystallin does not affect the lenticular concentrations of those nucleotides which are not specifically bound. The possibility that nucleotide binding may be a factor in the selection of some enzymes to serve as enzyme/crystallins is considered.

Full Text

Duke Authors

Cited Authors

  • Zigler, JS; Rao, PV

Published Date

  • February 1991

Published In

Volume / Issue

  • 5 / 2

Start / End Page

  • 223 - 225

PubMed ID

  • 2004667

Pubmed Central ID

  • 2004667

International Standard Serial Number (ISSN)

  • 0892-6638

Digital Object Identifier (DOI)

  • 10.1096/fasebj.5.2.2004667

Language

  • eng

Conference Location

  • United States