Differences in kinetic properties of cytochrome oxidase in mitochondria from rat tissues. A comparative study.
Substrate kinetic properties of cytochrome oxidase in rat liver, kidney, brain and heart mitochondria were examined using ascorbate + N,N,N',N'-tetramethyl-p-phenylenediamine (TMPD) as the electron donor system. Analysis of the substrate kinetics data revealed tissue-specific expression of kinetic components exhibiting differences with respect to Km, Vmax and Kcat/Km values. Regression analysis data suggest that the enzyme activity may be regulated in a tissue-specific manner.
Patel
Samir P
SP
Department of Biochemistry, Faculty of Science, The Maharaja Sayajirao University of Baroda, Vadodara, Gujarat, India.
Katyare
Surendra S
SS
D000818:Animals; D001921:Brain / Q000201:enzymology*; D003580:Cytochromes / Q000378:metabolism*; D003576:Electron Transport Complex IV / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008297:Male; D008928:Mitochondria / Q000201:enzymology*; D008929:Mitochondria, Heart / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D010743:Phospholipids / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
D003580:Cytochromes; D010743:Phospholipids; D003576:Electron Transport Complex IV