Evidence for the existence of tissue specific isoenzymes of mitochondrial NADH dehydrogenase.
Mitochondrial NADH dehydrogenase from a variety of rat tissues was isolated by immunoprecipitation with an antiserum to the bovine heart enzyme. The subunit composition of the enzyme from liver, kidney and lung differed from that present in heart, brain and skeletal muscle by the absence of an Mr 18,500 protein and the absence of an Mr 17,000 protein, suggesting the existence of tissue-specific isoenzymes.
Clay
V J
VJ
Department of Biochemistry, University of Southampton, U.K.
Ragan
C I
CI
D000818:Animals; D001921:Brain / Q000201:enzymology / Q000648:ultrastructure; D002417:Cattle; D003579:Cytochrome Reductases / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D007163:Immunosorbent Techniques; D007527:Isoenzymes / Q000032:analysis*; D007668:Kidney / Q000201:enzymology / Q000648:ultrastructure; D008168:Lung / Q000201:enzymology / Q000648:ultrastructure; D008928:Mitochondria / Q000201:enzymology*; D008929:Mitochondria, Heart / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology; D008931:Mitochondria, Muscle / Q000201:enzymology; D008970:Molecular Weight; D009245:NADH Dehydrogenase / Q000032:analysis*; D051381:Rats; D013367:Submitochondrial Particles / Q000201:enzymology
D007527:Isoenzymes; D003579:Cytochrome Reductases; D009245:NADH Dehydrogenase