ABSTRACT
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 5.2, and no detectable subunits. No iron, copper, manganese or molybdenium could be detected. On the basis of a minimum molecular mass of 72.5 kDa a ratio of FAD/protein of 1:1 could be derived. Its amino-acid composition, the light absorption and the fluorescence spectra are presented.
Subject(s)
Cytochrome Reductases/isolation & purification , Flavin-Adenine Dinucleotide/metabolism , Mycoplasma/enzymology , NADH Dehydrogenase/isolation & purification , Amino Acids/analysis , Catalysis , Chromatography, Gel , Chromatography, Ion Exchange , Electrophoresis, Polyacrylamide Gel , Kinetics , NADH Dehydrogenase/metabolism , Spectrometry, FluorescenceABSTRACT
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.
