Spectrophotometric detection of the interaction between cytochrome c and heparin
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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.
- MeSH
- chromatografie afinitní MeSH
- cytochromy skupiny c chemie metabolismus MeSH
- enzymy imobilizované MeSH
- heparin metabolismus MeSH
- oxidace-redukce MeSH
- polylysin farmakologie MeSH
- respirační komplex IV antagonisté a inhibitory metabolismus MeSH
- spektrální analýza MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- cytochromy skupiny c MeSH
- enzymy imobilizované MeSH
- heparin MeSH
- polylysin MeSH
- respirační komplex IV MeSH