Analysis of NADH dehydrogenases from plant [mung bean (Phaseolus aureus)] mitochondrial membranes on non-denaturing polyacrylamide gels and purification of complex I by band excision.
The present paper describes the analysis of plant mitochondrial NADH dehydrogenases using a recently developed non-dissociating gradient polyacrylamide-gel-electrophoresis technique [Kuonen, Roberts & Cottingham (1986) Anal. Biochem. 153, 221-226]. Solubilized mung-bean (Phaseolus aureus) submitochondrial particles were analysed on 3-22% (w/v) gradient polyacrylamide gels containing 0.1% Triton X-100 and stained for multiple NADH dehydrogenase activities. A rotenone-sensitive NADH dehydrogenase (Complex I) was identified on the basis of co-migration with the purified mammalian enzyme. The polypeptide composition of the plant enzyme was further analysed by band excision and SDS/polyacrylamide-gel electrophoresis.
Cottingham
I R
IR
Department of Biochemistry, University of Sussex, Brighton, U.K.
Moore
A L
AL
D003579:Cytochrome Reductases / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D007887:Fabaceae / Q000201:enzymology*; D007425:Intracellular Membranes / Q000201:enzymology; D007527:Isoenzymes / Q000032:analysis* / Q000302:isolation & purification; D009245:NADH Dehydrogenase / Q000032:analysis* / Q000302:isolation & purification; D010946:Plants, Medicinal; D013367:Submitochondrial Particles / Q000201:enzymology
D007527:Isoenzymes; D003579:Cytochrome Reductases; D009245:NADH Dehydrogenase