30398
Cytochrome c from bovine heart
≥95% (GE)
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About This Item
Form:
powder or crystals
Assay:
≥95% (GE)
Biological source:
bovine heart
biological source
bovine heart
assay
≥95% (GE)
form
powder or crystals
Quality Level
Gene Information
cow ... CYCS(510767)
technique(s)
activity assay: suitable
impurities
≤5% cytochrome c reduced
solubility
H2O: 10 mg/mL, clear, dark red-brown
UniProt accession no.
storage temp.
−20°C
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Preparation Note
Prepared by a procedure using TCA.
Other Notes
Sales restrictions may apply.
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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Why is the reduction of NO in cytochrome c dependent nitric oxide reductase (cNOR) not electrogenic?
Margareta R A Blomberg et al.
Biochimica et biophysica acta, 1827(7), 826-833 (2013-04-27)
The membrane-bound enzyme cNOR (cytochrome c dependent nitric oxide reductase) catalyzes the reduction of NO in a non-electrogenic process. This is in contrast to the reduction of O2 in cytochrome c oxidase (CcO), the other member of the heme-copper oxidase
Alexander N Volkov et al.
Biochemistry, 52(13), 2165-2175 (2013-03-23)
Here we present the preparation, biophysical characterization, and nuclear magnetic resonance (NMR) spectroscopy study of yeast cytochrome c peroxidase (CcP) constructs with enhanced solubility. Using a high-yield Escherichia coli expression system, we routinely produced uniformly labeled [(2)H,(13)C,(15)N]CcP samples with high
M Harjai et al.
Anaesthesia and intensive care, 41(2), 175-183 (2013-03-28)
Sepsis remains as a leading cause of death in critically ill patients. Unfortunately, there have been very few successful specific therapeutic agents that can significantly reduce the attributable mortality and morbidity of sepsis. Developing novel therapeutic strategies to improve outcomes
Esther Lapuente-Brun et al.
Science (New York, N.Y.), 340(6140), 1567-1570 (2013-07-03)
The textbook description of mitochondrial respiratory complexes (RCs) views them as free-moving entities linked by the mobile carriers coenzyme Q (CoQ) and cytochrome c (cyt c). This model (known as the fluid model) is challenged by the proposal that all
Eva Di Silvio et al.
Biochimica et biophysica acta, 1834(8), 1554-1561 (2013-05-08)
The biogenesis of c-type cytochromes (Cytc) is a process that in Gram-negative bacteria demands the coordinated action of different periplasmic proteins (CcmA-I), whose specific roles are still being investigated. Activities of Ccm proteins span from the chaperoning of heme b
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