Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1984-4-11
pubmed:abstractText
The interaction between bepridil and mitochondrial cytochrome c oxidase has been studied using the purified enzyme either in aqueous suspensions in the presence of detergents, or embedded into phospholipid vesicles. The investigation, systematically extended to nonactin and valinomycin for comparison, showed that: (a) valinomycin and nonactin induce similar changes in the visible absorption spectrum of cytochrome oxidase; these changes are quite different from those induced by bepridil. (b) The three compounds have an effect on the functional properties of purified, solubilized oxidase which may be related to binding. In particular, bepridil displays a complex pH-dependent effect which at concentrations below 50 microM results in a stimulation of the activity of approximately 30% starting with the oxidized resting enzyme. At variance with valinomycin and nonactin, the stimulatory effect is the same, within the errors, for the detergent-suspended, the vesicle-embedded and even the Keilin-Hartree particles. (c) In the case of detergent-suspended oxidase, the stimulatory effect of bepridil is also similar whether the enzyme is in the resting or in the pulsed state. If the oxidase is embedded into vesicles, however, the pulsed state is significantly more sensitive to bepridil than the resting one. These results are discussed in the light of the possible role assigned to pulsed oxidase in the regulation of the electron flux through the respiratory chain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
109-13
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Effect of bepridil on the activity of cytochrome c oxidase in solution and in proteoliposomes.
pubmed:publicationType
Journal Article