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

Authors


Abstract

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.

Ancillary