CHEMICAL STUDIES OF SEVERAL VARIETIES OF HB M

Abstract
Five different varieties of abnormal hemoglobin of the Hb M group have been examined and an amino acid sequence alteration detected in four. The anomalous spectroscopic behavior of the Hbs M could be explained by assuming the existence of a new reactive side group capable of complexing with the heme iron. The new substituents observed all have the necessary properties to form such an internal complex.