Prosimian hemoglobins: IV. The structural difference responsible for the hemoglobin phenotype of Lemur catta

The ring‐tailed lemur, Lemur catta, shows a two‐component hemoglobin phenotype after alkaline electrophoresis. A difference in the amino acid sequence of the isolated α‐globins was observed at position 15 (α I‐Gly, α II‐Lys) and can account for the electrophoretic pattern of two hemoglobin components. Only one other amino acid difference was found in the sequence of the two globin chains: a neutral substitution occurs at position 53 (α I‐Gly, α II‐Ala). The complete primary structures of the duplicated α‐globin chains of Lemur catta are presented.