Microbial lipoamide dehydrogenase. Purification and some characteristics of the enzyme derived from selected microorganisms.

摘要: Abstract 1. Lipoamide dehydrogenase (NADH:lipoamide oxidoreductase, EC 1.6.4.3) was partially purified from selected prokaryotic and eukaryotic organisms. The enzymes these sources were found to differ in their sensitivity inhibition by NADH. Serratia marcescens , like the enzyme Escherichia coli failed catalyse a significant initial reduction of lipoamide NADH absence added NAD + . This may be overcome prior addition reaction medium. In contrast, isolated Pseudomonas fluorescens, Bacillus subtilis Azotobacter agilis unaffected substrate levels enzymatic activity unchanged Eukaryotic inhibited NADH, but lesser extent than E. Coli or S. Marcescens 2. Saccharomyces cerevisiae Neurospora crassa displayed electrophoretic heterogeneity, having at least three diaphorase-reactive bands. prokaryotes formed either single band predominant upon electrophoresis. Molecular weights organisms estimated gel filtration polyacrylamide molecular both 110 000 ± 4400.