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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Detalhes bibliográficos
Main Authors: 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
Formato: Artigo
Idioma:Inglês
Publicado em: National Academy of Sciences 2005
Assuntos:
Biological Sciences
Acesso em linha: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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