Sequential inactivation of ζ-crystallin by o-phthalaldehyde

Author:

Bazzi Mohammad D.,Rabbani Nayyar,Duhaiman Ali S.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference28 articles.

1. Identification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase;Rao;J. Biol. Chem.,1992

2. Zeta-crystallin, a novel lens protein from the guinea pig;Huang;Curr. Eye Res.,1987

3. Zeta-crystallin is a major protein in the lens of Camelus dromedarius;Garland;Arch. Biochem. Biophys.,1991

4. Evidence for independent recruitment of zeta-crystallin/quinone reductase (CRYZ) as a crystallin in camelids and hystricomorph rodents;Gonzalez;Mol. Biol. Evol.,1995

5. High-affinity binding of NADPH to camel lens zeta-crystallin;Bazzi;Biochem. Biophys. Acta,2001

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