Cytochrome c from equine heart

Cytochrome c has been used:

• in the reduction of ferricytochrome c by xanthine oxidase-generated superoxide radicals
• as an analyte by the single droplet deposition method using MALDI mass spectra
• as a terminal electron acceptor in the assay of standard cytochrome c reductase activity
• in cytochrome c oxidase histochemistry
• in the measurement of cytochrome C oxidase activity
• as a component of phosphate buffer for the detection and evaluation of complex IV activity using blue-native gel electrophoresis (BN-PAGE)
• for detection of extracellular superoxide anion (ECSA) in isolated kidney phagocytes

The specific sites and extent of oxidation in horse cytochrome c treated with H₂O₂ and UV were characterized. It was suggested that the state of these sites could be used as a biomarker for the oxidative environment in a cell.

Cytochrome c, released from the outer mitochondrial compartment into the cytosol aids in activation of caspase-9 and initiation of the apoptotic protease cascade. This process is facilitated through its interaction with apoptotic protease-activating factor-1 (APAF-1) and deoxyadenosine triphosphate (dATP).(3) Various studies suggest that measurement of cytochrome C level in serum of tumor patients can be considered as a potential marker for cell death in vivo.

Cytochrome c is primarily known as an electron-carrying mitochondrial protein. The transition of cytochrome c between the ferrous and ferric states within the cell makes it an efficient biological electron-transporter and it plays a vital role in cellular oxidations in both plants and animals. It is generally regarded as a universal catalyst of respiration, forming an essential electron-bridge between the respirable substrates and oxygen

Prepared using TCA.

This product in solution should be dark red to reddish brown when dissolved in water at 10 mg/mL.

View more information on cytochrome c and electron transport at www.sigma-aldrich.com/enzymeexplorer.