C7150
Cytochrome c from equine heart
BioReagent, suitable for GFC marker
Synonym(s):
Cytochrome c from horse heart
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About This Item
Form:
powder
Mol wt:
~12,400
product line
BioReagent
Quality Level
form
powder
mol wt
~12,400
packaging
vial of ≥10 mg
suitability
suitable for GFC marker
storage temp.
−20°C
Application
Cytochrome c is primarily known as an electron-carrying mitochondrial protein and is generally regarded as a universal catalyst of respiration. Cytochrome c can be used as a gel filtration molecular weight marker in gel filtration chromatography and protein chromatography and can be used to study cytochrome c control proteins, electron transport and cellular respiration.
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 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
Other Notes
View more information on cytochrome c and electron transport at www.sigma-aldrich.com/enzymeexplorer.
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Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Protocols
Gel Filtration Markers Kit for Protein Molecular Weights 12,000-200,000 Da
Gel filtration chromatography is an established method for determining the size and molecular mass of proteins.
Federica Sinibaldi et al.
Journal of inorganic biochemistry, 105(11), 1365-1372 (2011-09-29)
In cells a portion of cytochrome c (cyt c) (15-20%) is tightly bound to cardiolipin (CL), one of the phospholipids constituting the mitochondrial membrane. The CL-bound protein, which has nonnative tertiary structure, altered heme pocket, and disrupted Fe(III)-M80 axial bond
Paolo Ascenzi et al.
Biochemical and biophysical research communications, 415(3), 463-467 (2011-11-08)
Carboxymethylation of equine heart cytochrome c (cytc) changes its tertiary structure by disrupting the heme-Fe-Met80 distal bond, such that carboxymethylated cytc (CM-cytc) displays myoglobin-like properties. Here, the effect of cardiolipin (CL) on peroxynitrite isomerization by ferric CM-cytc (CM-cytc-Fe(III)) is reported.
Kelly Watters et al.
PLoS pathogens, 14(12), e1007477-e1007477 (2018-12-12)
Viruses in the rhinovirus C species (RV-C) are more likely to cause severe wheezing illnesses and asthma exacerbations in children than related isolates of the RV-A or RV-B. The RV-C capsid is structurally distinct from other rhinoviruses and does not
Global Trade Item Number
| SKU | GTIN |
|---|---|
| C7150-1VL | 04061835572311 |
| C7150-5X1VL | 04061833295977 |