Spectrophotometric detection of the interaction between cytochrome c and heparin
Language English Country Netherlands Media print
Document type Journal Article
PubMed
1319206
DOI
10.1016/0005-2728(92)90076-e
PII: 0005-2728(92)90076-E
Knihovny.cz E-resources
- MeSH
- Chromatography, Affinity MeSH
- Cytochrome c Group chemistry metabolism MeSH
- Enzymes, Immobilized MeSH
- Heparin metabolism MeSH
- Oxidation-Reduction MeSH
- Polylysine pharmacology MeSH
- Electron Transport Complex IV antagonists & inhibitors metabolism MeSH
- Spectrum Analysis MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Cytochrome c Group MeSH
- Enzymes, Immobilized MeSH
- Heparin MeSH
- Polylysine MeSH
- Electron Transport Complex IV MeSH
Heparin inhibits transport of electrons from reduced cytochrome c to cytochrome c oxidase. The effect is due to the interaction of heparin with cytochrome c. It has been observed that binding of heparin to the reduced or oxidized cytochrome c changes the spectrum of cytochrome c at the Soret region. Affinity chromatography of heparin in cytochrome c immobilized to thiol-Sepharose shows that commercial heparin is eluted in the low-affinity and high-affinity fractions. Both participate in the interaction with cytochrome c. Polylysine induces decay of the cytochrome c-heparin complex.
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