Hemoglobin conformation couples erythrocyte S-nitrosothiol content to O(2) gradients

It is proposed that the bond between nitric oxide (NO) and the Hb thiol Cys-β(93) (SNOHb) is favored when hemoglobin (Hb) is in the relaxed (R, oxygenated) conformation, and that deoxygenation to tense (T) state destabilizes the SNOHb bond, allowing transfer of NO from Hb to form other (vasoactive)...

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Hlavní autoři: Doctor, Allan, Platt, Ruth, Sheram, Mary Lynn, Eischeid, Anne, McMahon, Timothy, Maxey, Thomas, Doherty, Joseph, Axelrod, Mark, Kline, Jaclyn, Gurka, Matthew, Gow, Andrew, Gaston, Benjamin
Médium: Artigo
Jazyk:Inglês
Vydáno: National Academy of Sciences 2005
Témata:
Biological Sciences
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC556285/
https://ncbi.nlm.nih.gov/pubmed/15824313
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0407490102
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