Abstract
Circular Dichroism (CD) of hemoglobin and its derivatives (including abnormal hemoglobin) was investigated. It is difficult to distinguish HbA, its α, β chains and myoglobin of horse heart from each other in absorption spectrum, but it can easily be accomplished in CD except between α chains and myoglobin. Peaks of CD of deoxygenated HbA are greater than the arithmetic mean of those of isolated chains, especially in the Soret region. The phenomenon could be considered as a representation of heme-heme interaction. As an example of application of CD on abnormal hemoglobin, we investigated CD of Hb Rainier α2β2145Tyr→Gys2145 TyrCys, an abnormal hemoglobin with diminished cooperativity. In the deoxygenated form of Hb Rainier, ellipticity at 433 nm is smaller than that of HbA. For the study of abnormal hemoglobins, especially for those with altered functions, usefulness of CD is suggested
