Purification and properties of an FAD-containing NADH oxidase from Mycoplasma capricolum.

From the prokaryotic microorganism Mycoplasma capricolum an FAD-containing NADH oxidase has been purified by preparative FPLC to homogeneity, as judged by polyacrylamide gel electrophoresis. The apparent molecular mass of the enzyme was found to be 72.5 kDa, with an isoelectric point of 5.

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

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.