ζ-Crystallin from guinea pig lens is capable of functioning catalytically as an oxidoreductase

P. Vasantha Rao, J. Samuel Zigler

Research output: Contribution to journalArticlepeer-review

Abstract

ζ-Crystallin, a major taxon-specific protein of the guinea pig lens, has been shown to be distantly related to the alcohol/polyol dehydrogenase family and to specifically bind NADPH. The capacity of ζ-crystallin to function catalytically was investigated in the present study. ζ-Crystallin exhibited an NADPH-dependent oxidoreductase activity with 2,6-dichlorophenolindophenol (DCIP). The NADPH:DCIP oxidoreductase activity of ζ-crystallin exhibits a linear response with increasing protein concentration, and saturation kinetics with NADPH and DCIP. This activity was abolished by heat inactivation and immunoadsorption of the protein. Dicumarol, Cibacron blue, manganese, and sulfhydryl reagents were inhibitory.

Original languageEnglish (US)
Pages (from-to)181-185
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume284
Issue number1
DOIs
StatePublished - Jan 1991

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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