Purification and Characterization of Superoxide Dismutase from Martianus Dermestoides Chevrola
Sephadex
Ion chromatography
Specific activity
Sepharose
Dismutase
DOI:
10.4028/www.scientific.net/amr.773.336
Publication Date:
2013-09-04T12:31:00Z
AUTHORS (6)
ABSTRACT
In this paper, the superoxide dismutase from Martianus dermestoides is purified by following methods: heat treatment, polyethylene concentration, Sephadex G-75 gel filtration, and DEAE-Sepharose FF ion exchange chromatography. The result shows that purification multiple 3.86, activation yield 21.89% specific of enzyme 447.6 U/mg. SOD appears to be a sole protein on SDS-PAGE molecular weight estimated 40.58 kDa. H 2 O can obviously inhibit CHCl 3 -CH CH OH only demonstrates basically no inhibitory effect. type might Cu/Zn-SOD. After purification, some enzymatic characterizations are studied. optimum reaction temperature 50°C. pH value 6. dermestoide has preferable stability below 50°C at values between 5-8.
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