An Origin of Cooperative Oxygen Binding of Human Adult Hemoglobin: Different Roles of the α and β Subunits in the α2β2 Tetramer
Fig 6
600 MHz 1H NMR spectra of Hb A, rHb(αH87G) and rHb(βH92G) in the deoxy-form.
Spectra are between 10 and 30 ppm at pH 7.0 and 25°C. The hemoglobin concentrations of Hb A, rHb(αH87G) an rHb(βH92G) were 1 mM, 800 and 500 μM, respectively, on a heme basis in 0.05 M phosphate buffer (pH 7.0). In addition, rHb(αH87G) and rHb(βH92G) contained 10 mM imidazole.