Identification of human hemoglobins.

IFFERENCES IN THE HEMOGLOBINS of the adult and the newborn have been recognized since 1866 (36). Rapid advances in this field, however, began in 1949, when Pauling and Itano (25) discovered that the hemoglobin of sickle cell disease differs from adult hemoglobin. Since that time, 8 hemoglobins have been identified, hemoglobin C (18) in 1950, hemoglobin D (14) in 1951, hemoglobin E (7, 17) and hemoglobin G (10) in 1954, and hemoglobin H (24, 28) in 1955. Hemoglobin I was described by Rucknagel and coworkers (30) in 1955, hemoglobin J by Battle and Lewis (2) in 1954. The hemoglobin listed as K by Allison (1) carries the designation J in the review of Itano (16), and is further described by Thorup (1, 16). The heterogeneity of normal adult hemoglobin as manifested by its electrophoretic behavior was first described by Derrien (9) in 1953. Studies by Kunkel and Wallenius (19), and Shavit and Brener (31) supported this finding. Morrison and Cook (22) observed the heterogeneity of hemoglobin A by chromatography on an ion-exchange resin. More recently Cook and Morrison (8) have found hemoglobin F to he heterogeneous as well. The alkali-resistant hemoglobin present in normal adults in very small amounts appears to be identical with fetal hemoglobin in amino acid composition according to studies made by Huisman et al. (12). Van der Schaaf and Huisman (34) have found that the alkali-resistant component present in some patients with sickle cell anemia differs from fetal hemoglobin in ultraviolet absorption spectra and amino acid composition. Excellent reviews on the present status of the human hemoglobins by Chernoff (4, 5, 6) and Itano (16) have appeared in 1955.