FIG. 1.

PAGE of the purified aldehyde dehydrogenase complex from Ga. diazotrophicus. (a) Approximately 50 μg of purified protein was loaded on native gel (10%) and stained by Coomassie brilliant blue. (b) Aldehyde dehydrogenase activity was stained by zymography. Alternatively, the purified enzyme (50 μg of protein) was subjected to SDS-PAGE and first stained by the peroxidase assay with tetramethylbenzidine (c), followed by the Coomassie blue stain (d). The molecular mass of each band is indicated on the side in kilodaltons. The electrophoresis procedures and stain techniques are described in Materials and Methods.