Spectrophotometric detection of the interaction between cytochrome c and heparin

. 1992 May 20 ; 1100 (2) : 155-9.

Jazyk angličtina Země Nizozemsko Médium print

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/pmid01319206
Odkazy

PubMed 1319206
DOI 10.1016/0005-2728(92)90076-e
PII: 0005-2728(92)90076-E
Knihovny.cz E-zdroje

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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