Structural relationships between the NADH dehydrogenases of Paracoccus denitrificans and bovine heart mitochondria as revealed by immunological cross-reactivities.
An antibody raised against two subunits (Mr 48 000 and 25 000) of NADH dehydrogenase from Paracoccus denitrificans cross-reacts with one of more than 20 polypeptides that form the bovine heart mitochondrial NADH dehydrogenase. The cross-reacting subunit has Mr 51 000 and is believed to be the NADH-binding subunit of the enzyme. Antibodies raised against certain subunits of the bovine heart NADH dehydrogenase were tested for cross-reactivity with P. denitrificans cytoplasmic membranes. Of those tested, only one, an antibody specific for the 49 kDa subunit of mitochondrial NADH dehydrogenase, cross-reacted with the bacterial membranes. It recognised a polypeptide of approximate Mr 46 000. This is an indication for a previously undetected third subunit of NADH dehydrogenase from P. denitrificans. The immunological cross-reactions indicate that the NADH dehydrogenases from P. denitrificans and bovine heart mitochondria are related structurally.
D000818:Animals; D002417:Cattle; D003429:Cross Reactions; D003579:Cytochrome Reductases / Q000032:analysis*; D008929:Mitochondria, Heart / Q000201:enzymology*; D008970:Molecular Weight; D009245:NADH Dehydrogenase / Q000032:analysis* / Q000276:immunology; D010231:Paracoccus denitrificans / Q000201:enzymology*
D003579:Cytochrome Reductases; D009245:NADH Dehydrogenase