The emission spectra of human adult hemoglobin A0 and its isolated α and ß subunits were obtained using a highly sensitive photon‐counting spectrofluorometer. The quantum yields of the emissions, relative to free tryptophan, were also measured as well as the excitation polarization spectra for hemoglobin A0 and apohemoglobin. The fluorophore bis‐ANS was utilized to probe for the presence of apoproteins in the hemoprotein preparations. The work suggests that tryptophan may be useful as an intrinsic probe to study dynamical processes in hemoglobin.
No takes yet. Share an insight, caveat, or question.
Alpert et al. (1980) studied this question.
Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context: