Hemoglobin H Associated with an Uncommon Variant of Thalassemia Trait

discovery of a new hemoglobin characterized electrophoretically at pH 8.6 by a more rapid anodal mobility than that of normal adult hemoglobin. This hemoglobin has subsequently been identified by the letter “H. ” More recently, “fast ” hemoglobins other than “H ” have been described. These include hemoglobins J,3 J,4-1#{176}K,5-13 N’3 and two others found in infants but not identified by letters.13”4 The anodal migration rate of hemoglobin H, on paper electrophoresis at pH 8.6, is distinct from all others except hemoglobin I. At pH 6.5 the anodal migra-tion of hemoglobin H distinguishes it from hemoglobin I. The spontaneous denaturation of hemoglobin I-I within intact erythrocytes in vitro, results in the formation of multiple inclusion bodies. This process, which is accelerated by the incubation of red cells at 37 C. with brillant cresyl blue, or with the reducing agent, sodium dithionite, results in a characteristic appearance which is sufficient to enable detection of the anomaly.2 The familial transmission of most abnormal hemoglobins has been illustrate