Molecular cloning and sequencing of ζ-crystallin/quinone reductase cDNA from human liver

Pedro Gonzalez, P. Vasantha Rao, J. Samuel Zigler

Research output: Contribution to journalArticlepeer-review

Abstract

Zeta-crystallin is an enzyme-crystallin highly expressed in the lens of some hystricomorph rodents and camels. It has been shown to have a novel NADPH:quinone oxidoreductase activity and is present at enzymatic levels in a variety of tissues from various mammals. We report here the cDNA cloning of ζ-crystallin from a human liver library. One clone with the complete open reading frame was obtained. Ten nucleotides of the 5′ and 796 of the 3′ non-translated regions are present in the clone including two possible polyadenylation signals. The deduced amino acid sequence is 328 residues long with a calculated molecular mass of 34910 daltons and isoelectric point of 8.73. It shows 84% identity with the guinea pig protein.

Original languageEnglish (US)
Pages (from-to)902-907
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume191
Issue number3
DOIs
StatePublished - Mar 31 1993

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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