Carbon Monoxide Binding in a Model of Hemoglobin Differs Between the T and the R Conformation

Autor:	Zock, Jacob P., Piiper, J, Goldstick, TK, Meyer, M
Jazyk:	angličtina
Rok vydání:	1990
Předmět:	chemistry.chemical_compound chemistry Stereochemistry Competitive binding Physical chemistry chemistry.chemical_element Carbon monoxide binding Hemoglobin Saturation (chemistry) Oxygen affinity Oxygen Oxygen binding Carbon monoxide
Zdroj:	Oxygen Transport to Tissue XII, 199-207 STARTPAGE=199;ENDPAGE=207;TITLE=Oxygen Transport to Tissue XII Advances in Experimental Medicine and Biology ISBN: 9781468481839
DOI:	10.1007/978-1-4684-8181-5_25
Popis:	Carbon monoxide impedes the transport of oxygen in blood by competitive binding to the oxygen binding sites on hemoglobin. The affinity of these sites for carbon monoxide is much greater than that for oxygen. The ratio between carbon monoxide affinity and oxygen affinity (M) is usually assumed to have a fixed value (Haldane’s law), which is about 200. Reported values differ between authors (Douglas et al., 1912, Killick, 1936, Sendroy et al., 1929). However, this ratio is not a constant but depends on the level of saturation (Roughton, 1970) as well as on pH (Joels and Pugh, 1958). This means that simple procedures cannot be used to calculate the combined effects of simultaneous oxygen and carbon monoxide binding. Application of our mathematical model of hemoglobin (Zock, 1987) shows that this model can account for the above-mentioned phenomena in a straightforward way.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2f015c272eb294920a0221b8e585695 https://doi.org/10.1007/978-1-4684-8181-5_25 Zobrazit plný text záznamu