Peroxidase from Astragalus maritimus: purification and properties.
A peroxidase has been purified to homogeneity from Astragalus maritimus seeds using ammonium sulfate precipitation and chromatography on DEAE-cellulose and hydroxylapatite. The purification obtained was 255 fold. The enzyme preparations were homogenous by the criteria of SDS-PAGE and analytical gel electrofocusing. The protein contained 0.11% of iron that corresponds to a minimum molecular size of 50,700. Determinations of molecular size by SDS-PAGE gave values of 48,000 +/- 1,000 while the one obtained by Sephadex gel filtration was 49,000. The pH optimum of the enzyme was 6.0. The activation energy was estimated to be 6 Kcal/mol. The prosthetic group was shown to be ferriprotoporphyrin IX. The presence of 13% neutral sugars was found. The spectrophotometric analysis showed the presence, in the visible region, of absorption maxima at 403, 490 and 633 nm. The Rz value (A403/A275) was 2.7.
Cogoni
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A
Istituto di Chimica Biologica, Università, Cagliari.
Medda
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R
Saba
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L
Floris
G
G
D007887:Fabaceae / Q000201:enzymology*; D010544:Peroxidases / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D010946:Plants, Medicinal
D010544:Peroxidases