Reinards R, Altdorf R, Ohlenbusch H D
Hoppe Seylers Z Physiol Chem. 1984 May;365(5):577-85. doi: 10.1515/bchm2.1984.365.1.577.
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.
从原核微生物莱氏无胆甾原体中，主要的含锰超氧化物歧化酶已被纯化至同质，这通过聚丙烯酰胺凝胶电泳判断。该酶的分子量为41500道尔顿。它由两个大小相同的亚基组成，等电点为6.4。每个亚基含有0.51±0.05个锰原子。给出了其氨基酸组成和光吸收光谱，并与来自其他原核生物的含锰和含铁超氧化物歧化酶进行了比较。
