| pubmed-article:10954746 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10954746 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:10954746 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:10954746 | lifeskim:mentions | umls-concept:C0028128 | lld:lifeskim |
| pubmed-article:10954746 | lifeskim:mentions | umls-concept:C0005775 | lld:lifeskim |
| pubmed-article:10954746 | lifeskim:mentions | umls-concept:C0025519 | lld:lifeskim |
| pubmed-article:10954746 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
| pubmed-article:10954746 | lifeskim:mentions | umls-concept:C0028198 | lld:lifeskim |
| pubmed-article:10954746 | lifeskim:mentions | umls-concept:C0019046 | lld:lifeskim |
| pubmed-article:10954746 | lifeskim:mentions | umls-concept:C0205345 | lld:lifeskim |
| pubmed-article:10954746 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
| pubmed-article:10954746 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:10954746 | pubmed:dateCreated | 2000-10-5 | lld:pubmed |
| pubmed-article:10954746 | pubmed:abstractText | To quantify the reactions of nitric oxide (NO) with hemoglobin under physiological conditions and to test models of NO transport on hemoglobin, we have developed an assay to measure NO-hemoglobin reaction products in normal volunteers, under basal conditions and during NO inhalation. NO inhalation markedly raised total nitrosylated hemoglobin levels, with a significant arterial-venous gradient, supporting a role for hemoglobin in the transport and delivery of NO. The predominant species accounting for this arterial-venous gradient is nitrosyl(heme)hemoglobin. NO breathing increases S-nitrosation of hemoglobin beta-chain cysteine 93, however only to a fraction of the level of nitrosyl(heme)hemoglobin and without a detectable arterial-venous gradient. A strong correlation between methemoglobin and plasma nitrate formation was observed, suggesting that NO metabolism is a primary physiological cause of hemoglobin oxidation. Our results demonstrate that NO-heme reaction pathways predominate in vivo, NO binding to heme groups is a rapidly reversible process, and S-nitrosohemoglobin formation is probably not a primary transport mechanism for NO but may facilitate NO release from heme. | lld:pubmed |
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| pubmed-article:10954746 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10954746 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10954746 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10954746 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10954746 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:10954746 | pubmed:author | pubmed-author:SchechterA... | lld:pubmed |
| pubmed-article:10954746 | pubmed:author | pubmed-author:NicholsJ SJS | lld:pubmed |
| pubmed-article:10954746 | pubmed:author | pubmed-author:ShelhamerJ... | lld:pubmed |
| pubmed-article:10954746 | pubmed:author | pubmed-author:OgnibeneF PFP | lld:pubmed |
| pubmed-article:10954746 | pubmed:author | pubmed-author:PannellL KLK | lld:pubmed |
| pubmed-article:10954746 | pubmed:author | pubmed-author:GladwinM TMT | lld:pubmed |
| pubmed-article:10954746 | pubmed:author | pubmed-author:Pease-FyeM... | lld:pubmed |
| pubmed-article:10954746 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10954746 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:10954746 | pubmed:volume | 97 | lld:pubmed |
| pubmed-article:10954746 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10954746 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10954746 | pubmed:pagination | 9943-8 | lld:pubmed |
| pubmed-article:10954746 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:10954746 | pubmed:meshHeading | pubmed-meshheading:10954746... | lld:pubmed |
| pubmed-article:10954746 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10954746 | pubmed:articleTitle | Relative role of heme nitrosylation and beta-cysteine 93 nitrosation in the transport and metabolism of nitric oxide by hemoglobin in the human circulation. | lld:pubmed |
| pubmed-article:10954746 | pubmed:affiliation | Critical Care Medicine Department of the Warren G. Magnuson Clinical Center, National Institutes of Health, Bethesda, MD 20892, USA. mgladwin@nih.gov | lld:pubmed |
