Tissue- and species-specific expression of cytochrome c oxidase isozymes in vertebrates.
Cytochrome c oxidase was isolated from brown fat tissue of the rat and compared with the isozymes from rat liver and heart, which differ at least in subunits VIa and VIII. ELISA titrations of COX from the three tissues with monospecific antisera to all 13 subunits of the rat liver enzyme showed differences between the three enzymes. The N-terminal amino-acid sequence analysis of subunits VIa and VIII from SDS-PAGE gel bands of the three enzymes indicates the occurrence of three different isozymes in the rat. N-terminal amino-acid sequence analysis of subunits VIa and VIII from cytochrome c oxidase of bovine and human heart demonstrates also species-specific differences in the expression of the 'liver-type' and 'heart-type' of subunits VIa and VIII.
Kadenbach
B
B
Fachbereich Chemie, Biochemie der Philipps-Universität Marburg, F.R.G.
Stroh
A
A
Becker
A
A
Eckerskorn
C
C
Lottspeich
F
F
D002001:Adipose Tissue, Brown / Q000201:enzymology; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003080:Cold Temperature; D003576:Electron Transport Complex IV / Q000378:metabolism*; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism; D008929:Mitochondria, Heart / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D051381:Rats; D013045:Species Specificity; D014018:Tissue Distribution
D007527:Isoenzymes; D003576:Electron Transport Complex IV