Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 785-791 |
| Number of pages | 7 |
| Journal | Zeitschrift fur Naturforschung - Section C Journal of Biosciences |
| Volume | 60 |
| Issue number | 9-10 |
| DOIs | |
| State | Published - 2005 |
Keywords
- Cytochrome Content
- Cytochrome Oxidase
- Mitochondrial Phospholipids
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology
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