Spectrophotometric detection of the interaction between cytochrome c and heparin.
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.
Antalík
M
M
Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Czechoslovakia.
Bona
M
M
Gazová
Z
Z
Kuchár
A
A
D002846:Chromatography, Affinity; D003574:Cytochrome c Group / Q000737:chemistry / Q000378:metabolism*; D003576:Electron Transport Complex IV / Q000037:antagonists & inhibitors / Q000378:metabolism; D004800:Enzymes, Immobilized; D006493:Heparin / Q000378:metabolism*; D010084:Oxidation-Reduction; D011107:Polylysine / Q000494:pharmacology; D013057:Spectrum Analysis
D003574:Cytochrome c Group; D004800:Enzymes, Immobilized; D011107:Polylysine; D006493:Heparin; D003576:Electron Transport Complex IV