Direct measurement of carbon monoxide bound to different subunits of hemoglobin A in solution and in red cells by infrared spectroscopy.

Autor: Potter WT, Hazzard JH, Kawanishi S, Caughey WS
Jazyk: angličtina
Zdroj: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1983 Oct 31; Vol. 116 (2), pp. 719-25.
DOI: 10.1016/0006-291x(83)90584-3
Abstrakt: Infrared spectra for carbon monoxide bound to alpha and beta subunits of human hemoglobin A have subunit differences near 1950 cm-1 and indicate that 92% of the alpha subunits exist in one conformer and 5% in a second conformer under conditions where 99% of the beta subunit is in only one conformation. The sum of the separated subunit spectra is equivalent to the alpha 2 beta 2 tetramer spectrum. CO infrared spectra indicate that CO displaces O2 from HbO2 in red cells or in solution preferentially at the beta subunits. The measurement of C-O stretch bands provides a direct method for characterization of ligand binding sites within intact cells.
Databáze: MEDLINE