Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-5-1
pubmed:abstractText
The possibility of binding of CO to cytochrome c oxidase (cytochrome a,a3) in brain cortex has been examined in vivo by reflectance spectrophotometry. During ventilation with CO-containing gases, cytochrome a,a3 absorption at 605 nm increased in the parietal cortex of anesthetized rats during carboxyhemoglobin (HbCO) formation. HbCO levels, measured by changes in absorption at 569-586 nm in vivo, correlated positively with arterial HbCO by CO oximetry. Arterial blood pressure and calculated O2 content varied inversely with HbCO. During CO exposure, decreases in blood pressure, O2 content, and cytochrome a,a3 oxidation level could be reversed partly at constant HbCO by compression to 3 atmospheres absolute (ATA). After removing CO from inspired gas at 3 ATA, optical and physiological parameters recovered completely to control values except for minor persistent elevations of HbCO. Difference spectra from parallel experiments at constant HbCO revealed absorption minima at 588-592 nm and 600-605 nm as a result of hyperbaric exposure. Spectral analysis of these components was consistent with partial dissociation of a cytochrome a3-CO complex and cytochrome a reoxidation with increasing dissolved O2 in hyperbaric conditions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
8750-7587
pubmed:author
pubmed:issnType
Print
pubmed:volume
68
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
604-10
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
In vivo binding of carbon monoxide to cytochrome c oxidase in rat brain.
pubmed:affiliation
Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.