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 |
Externí odkaz: |
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