Molecular Weight of Native and Dissociated Cysteamine Oxygenase

Abstract

Cysteamine oxygenase has been further purified to a degree where it appeared homogeneous in disc gel electrophoresis. The purified enzyme possesses a molecular weight of 52000 when it is treated with either 8 M urea or with 0.1 % sodium dodecyl sulfate. The molecular weight of the native undissociated enzyme was 96000 when determined by dextran gel filtration and 92000 when determined by sedimentation equilibrium in the ultracentrifuge. These results are consistent with the occurrence of two similar subunits in the molecule of eysteamine oxygenase.