Stability of Cytochrome c at Extreme pH Values.
- 1 January 1948
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 2 (5-6) , 430-439
- https://doi.org/10.3891/acta.chem.scand.02-0430
Abstract
Cytochrome c was perfectly stable from pH 1.6 to 12.3, as determined by measuring its activity in an enzyme system, rather than spectroscopically. The presence or absence of hemin proteins in tissues could be proven with certainty by spectrochemical data only. An appearance of higher activity after treatment with acid or base was noted.Keywords
This publication has 6 references indexed in Scilit:
- THE EFFECTS OF CYTOCHROME c ON ANOXIC AND CYANIDE-POISONED RATSJournal of Biological Chemistry, 1947
- A COMPARATIVE STUDY OF THE BLOOD AND LIVER CATALASES FROM THE HORSE1947
- The inhibition of succinoxidase by heavy metals and its reactivation with dithiolsBiochemical Journal, 1947
- Activity of the cytochrome system in heart muscle preparationsBiochemical Journal, 1947
- Purification and properties of cytochrome cBiochemical Journal, 1945
- Succinic dehydrogenase-cytochrome system of cells intracellular respiratory system catalysing aerobic oxidation of succinic acidProceedings of the Royal Society of London. B. Biological Sciences, 1940