The abnormality of the primary structure of hemoglobin shimonoseki

Abstract

Received April2, 1965 In 1960 Yamaoka et al. described one of the first well-documented abnormal hemoglobins to be found in Japan. This hemoglobin, designated Hb Shimonoseki for the city in which the family resides, constitutes approximately 20% of the hemoglobin of the heterozygotes and migrates with Hb S on paper electrophoresis at pH 8.6. The present communication concerns its further characterization. On starch gel electrophoresis (Smithies, 1959), using borate buffer at pH 8.6, Hb Shimonoeeki migrated very slightly cathodally to Hb S, even when the hemolysates were adjusted so as to contain equal amounts of the abnormal components. On Amberlite CG-50 column chromatography (Allen et., 1958) the Hb Shimonoseki peak was eluted with 110 ml. of developer compared with 65 ml. for normal Hb A and 130 ml. for Hb S. Hybridization of Hb Shimonoseki with other hemoglobins known to have abnormal aor B-polypeptide chains was performed on starch gel using the technique of Singer and Itano (1959) demonstrating that the amino acid substitution resides in the a-chain. Normal adult hemoglobin (Hb A) and Hb Shimonoseki were separated and purified by starch block electrophoresis. Heat denatured hemoglobi solutions were digested with TCA trypsin and fingerprinted (Ingram,