HB Handa [alpha 90 (FG 2) Lys replaced by Met]: structure and biosynthesis of a new slightly higher oxygen affinity variant.
Hb Handa, an abnormal hemoglobin which isoelectrofocused anodally to Hb A, was found in a 15-year-old Japanese girl and her mother, who were apparently healthy. Clinical and hematological examinations showed no abnormality in individual heterozygous for this mutant gene except for a slight increase of reticulocyte count (2.1-2.4%). Structural studies disclosed an alpha chain anomaly and substitution of alpha 90 (FG 2) Lys replaced by Met. The content of the abnormal hemoglobin in the hemolysate was 17.5-18.3% of the hemoglobin. The isopropanol precipitation test was negative. The purified abnormal hemoglobin showed a slightly higher oxygen affinity than that of Hb A, but Hill's n constant, Bohr effect and organic phosphate effect were within the normal range. Globin chain biosynthesis in reticulocytes indicated that the production rate of the abnormal alpha chain was suppressed to 38% of the normal level.
D000293:Adolescent; D055598:Chemical Phenomena; D002621:Chemistry; D004588:Electrophoresis, Cellulose Acetate; D005260:Female; D006455:Hemoglobins, Abnormal / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification*; D006801:Humans; D007564:Japan; D008239:Lysine; D008706:Methemoglobin; D008715:Methionine; D010100:Oxygen / Q000097:blood*; D010108:Oxyhemoglobins
D006455:Hemoglobins, Abnormal; D010108:Oxyhemoglobins; C037846:hemoglobin Munakata; D008706:Methemoglobin; D008715:Methionine; D008239:Lysine; D010100:Oxygen