Literature DB >> 8784923

Purification and properties of Oryza sativa Cu-Zn superoxide dismutase.

A Padiglia1, R Medda, E Cruciani, A Lorrai, G Floris.   

Abstract

Superoxide dismutase has been purified to homogeneity from Oryza sativa germinated seeds growth in the dark. The purified enzyme contained two electrophoretically distinct bands on continuous gel electrophoresis or analytical gel electrofocusing. SDS-PAGE showed a single band of an M(r) 15000 while gel chromatography on Sephadex G 100 showed a single peak of an M(r) 32000. It contained two Cu and two Zn ions. The spectra of ultraviolet and visible regions were similar to those of Cu-Zn mammalian and plant superoxide dismutases. The activation energy was estimated at 16 Kcal mol-1.

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Year:  1996        PMID: 8784923     DOI: 10.1080/10826069608000059

Source DB:  PubMed          Journal:  Prep Biochem Biotechnol        ISSN: 1082-6068            Impact factor:   2.162


  2 in total

1.  Expression and characterization of monocot rice cytosolic CuZnSOD protein in dicot Arabidopsis.

Authors:  S M Pan; M K Chen; M H Chung; K W Lee; I C Chen
Journal:  Transgenic Res       Date:  2001-08       Impact factor: 2.788

2.  Use of a metallopeptide-based mimic provides evidence for a proton-coupled electron-transfer mechanism for superoxide reduction by nickel-containing superoxide dismutase.

Authors:  Jason Shearer
Journal:  Angew Chem Int Ed Engl       Date:  2013-01-22       Impact factor: 15.336

  2 in total

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