Purification and properties of a manganese-containing superoxide dismutase from Acholeplasma laidlawii.

R Reinards, R Altdorf, H D Ohlenbusch
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引用次数: 4

Abstract

From the prokaryotic microorganism Acholeplasma laidlawii the major manganese-containing superoxide dismutase has been purified to homogeneity, as judged by polyacrylamide gel electrophoresis. The molecular mass of the enzyme was found to be 41 500 Da. It consists of two subunits of identical size and has an isoelectric point of 6.4. The enzyme contains 0.51 +/- 0.05 atoms of manganese per subunit. Its amino-acid composition and light absorption spectra are presented and compared with Mn- and Fe- containing superoxide dismutases from other prokaryotic organisms.

一种含锰超氧化物歧化酶的纯化及性质研究。
通过聚丙烯酰胺凝胶电泳鉴定,从原核微生物莱氏革单胞体中纯化出主要的含锰超氧化物歧化酶。酶的分子量为41 500 Da。它由两个大小相同的亚基组成,等电点为6.4。这种酶每个亚基含有0.51 +/- 0.05个锰原子。介绍了其氨基酸组成和光吸收光谱,并与其他原核生物的含锰和含铁超氧化物歧化酶进行了比较。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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