Proteins of bacterial membranes. NADH-dehydrogenase from the cells of Acholeplasma laidlawii

Kapitanov, A.B.; Smirnova, M.N.; Kazennova, E.V.

Biokhimiia 47(11): 1867-1872

1982


ISSN/ISBN: 0320-9725
PMID: 7150675
Document Number: 183506
Using ion-exchange chromatography on DEAE-cellulose and gel filtration, a purified NADH-dehydrogenase was prepared from cell membranes of A. laidlawii. The enzyme specific activity exceeds the activity of the membrane preparation 45-fold. The enzyme is thermolabile and sensitive to lecithine. Electrophoresis of the enzyme preparation in the presence of Na-DS resulted in two proteins with Mr of 65 000 and 72 000. Specific staining of the gels with triphenyltetrasolium chloride in the presence of Triton X-100 revealed two protein bands, while in the presence of Triton X-100 and urea only one protein band was produced.

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