Purification and characterization of zeta-crystallin/quinone reductase from guinea pig liver.

Published

Journal Article

zeta-Crystallin, a major lens protein of certain mammalian species, has recently been characterized as a novel and active NADPH:quinone oxidoreductase. Here we report the purification of this protein from guinea pig liver by utilizing sequentially: ammonium sulphate precipitation, Blue Sepharose affinity, cation exchange and hydrophobic chromatography steps. This four-step isolation procedure yielded 118-fold purification and a specific activity of 6 U/mg protein when assayed in the presence of 9,10-phenanthrenequinone. Kinetic, immunological and physical properties of this protein have been found to be identical with those of guinea pig lens zeta-crystallin. Western blot analysis using antibodies raised against zeta-crystallin peptides demonstrated the presence of substantial amounts of this protein in human liver homogenates.

Full Text

Duke Authors

Cited Authors

  • Rao, PV; Zigler, JS

Published Date

  • October 27, 1992

Published In

Volume / Issue

  • 1117 / 3

Start / End Page

  • 315 - 320

PubMed ID

  • 1420281

Pubmed Central ID

  • 1420281

International Standard Serial Number (ISSN)

  • 0006-3002

Language

  • eng

Conference Location

  • Netherlands