Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-3-2
pubmed:abstractText
Shifts of the steady state of cytochromes a, a3 and c at high pO2 values are cited as evidence of the low O2 affinity of cytochrome oxidase in vivo [(1971) Brain Res. 108, 143-154; (1985) Adv. Exp. Med. Biol. 191, 833-842; (1987) in: Int. Soc. Oxygen Transp. Tissue, Sapporo, p. 84]. Highly aerobic, small diploid yeast cells show less than 0.44% change of steady state in the interval prior to an abrupt reduction of cytochrome c. Thus, 'pre-reduction' seems falsified as a physiological response of metabolizing yeast cells that are free of hemoglobin, do not aggregate and maintain a steady state. Pre-reduction may be due to spectroscopic interference, for example hemoglobin deoxygenation, to oxygen gradients in aggregated cells and tissues or to non-steady states of substrate and metabolic controls, as contrasted to an altered cytochrome oxidase oxygen affinity in vivo.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
226
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
343-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Early reduction of cytochrome c in hypoxia.
pubmed:affiliation
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.