Manganese superoxide dismutase from a higher plant : Purification of a new Mn-containing enzyme.

Abstract:

:A manganese-containing superoxide dismutase (EC 1.15.1.1) was purified to homogeneity from a higher plant for the first time. The enzyme was isolated fromPisum sativum leaf extracts by thermal fractionation, ammonium sulfate salting out, ion-exchange and gel-filtration column chromatography, and preparative polyacrylamide gel electrophoresis. Pure manganese superoxide dismutase had a specific activity of about 3,000 U mg(-1) and was purified 215-fold, with a yield of 1.2 mg enzyme per kg whole leaf. The manganese superoxide dismutase had a molecular weight of 94,000 and contained one g-atom of Mn per mol of enzyme. No iron and copper were detected. Activity reconstitution experiments with the pure enzyme ruled out the possibility of a manganese loss during the purification procedure. The stability of manganese superoxide dismutase at-20°C, 4°C, 25°C, 50°C, and 60°C was studied, and the enzyme was found more labile at high temperatures than bacterial manganese superoxide dismutases and iron superoxide dismutases from an algal and bacterial origin.

journal_name

Planta

journal_title

Planta

authors

Sevilla F,López-Gorgé J,Gómez M,Del Río LA

doi

10.1007/BF00582359

subject

Has Abstract

pub_date

1980-01-01 00:00:00

pages

153-7

issue

2

eissn

0032-0935

issn

1432-2048

journal_volume

150

pub_type

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