[Primary structure of abnormal E-like hemoglobin].

An E-like abnormal hemoglobin was detected in a hematological patient and one of the members of her family. The composition of blood hemolyzates was characterized using acetate cellulose electrophoresis. The abnormal beta-chain was isolated by ion-exchange chromatography of total globin on CM-cellulose. Using peptide mapping of the abnormal beta-chain trypsin hydrolysates, it was shown that the amino acid substitution occurs in peptide beta T3. The amino acid analysis and determination of the abnormal fragment C-terminal amino acid allowed to establish the locus and type of this substitution. The first case of hemoglobin E(alpha 2 beta 2 26Glu leads to Lys) identification on the territory of the USSR is reported.