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biological source
horse heart
Quality Level
assay
≥95% (SDS-PAGE)
form
powder
mol wt
12,384
technique(s)
cell based assay: suitable
solubility
H2O: soluble 10 mg/mL
suitability
suitable for molecular biology
UniProt accession no.
application(s)
cell analysis
storage temp.
−20°C
Gene Information
horse ... CYCS(100053958)
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Application
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.
Biochem/physiol Actions
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
Preparation Note
Prepared using TCA.
Other Notes
View more information on cytochrome c and electron transport at www.sigma-aldrich.com/enzymeexplorer.
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
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B C Hill
The Journal of biological chemistry, 266(4), 2219-2226 (1991-02-05)
The reaction of the electrostatic cytochrome c-cytochrome oxidase complex with oxygen is measured by transient absorption spectroscopy. The oxygen reaction is initiated by photolytic removal of CO from cytochrome oxidase, using a flash-pumped dye laser. The subsequent reaction of the
Vittorio Pandini et al.
The Journal of biological chemistry, 277(50), 48463-48471 (2002-10-09)
Toxoplasma gondii possesses an apicoplast-localized, plant-type ferredoxin-NADP(+) reductase. We have cloned a [2Fe-2S] ferredoxin from the same parasite to investigate the interplay of the two redox proteins. A detailed characterization of the two purified recombinant proteins, particularly as to their
Enzyme-catalyzed free radical reactions with nicotinamide adenine nucleotides. II. Lactate dehydrogenase-catalyzed oxidation of reduced nicotinamide adenine dinucleotide by superoxide radicals generated by xanthine oxidase.
P C Chan et al.
The Journal of biological chemistry, 249(4), 1317-1319 (1974-02-25)
A novel role of the mitochondrial permeability transition pore in (-)-gossypol-induced mitochondrial dysfunction
Warnsmann V, et al.
Mechanisms of Ageing and Development, 170, 45-58 (2018)
Rapid extracellular release of cytochrome c is specific for apoptosis and marks cell death in vivo
Renz A, et al.
Blood, 98(5), 1542-1548 (2001)
Chromatograms
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