FIG. 3.

Analysis of active and inactive XDH from R. capsulatus by polyacrylamide gel electrophoresis. Purified XDH was electrophoresed under nondenaturing conditions in 6% polyacrylamide gels and stained for protein with Coomassie brilliant blue. Arrows indicate different electrophoretic mobilities of active (lane 1 and 2) and inactive (lane 3) XDH. Lane 1, 2 μg of active XDH purified from R. capsulatus KS36; lane 2, 2 μg of active XDH purified from R. capsulatus R507 (moeA) grown in the presence of 1 mM molybdate; lane 3, 2 μg of inactive XDH purified from R. capsulatus R507 (moeA) grown without molybdate supplementation.