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Prosimian hemoglobins: IV. The structural difference responsible for the hemoglobin phenotype of Lemur catta
Author(s) -
Duffy Lawrence K.,
Ehrhardt Margaret M.,
BuettnerJanusch John,
Coppenhaver Dorian H.
Publication year - 1987
Publication title -
american journal of primatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.988
H-Index - 81
eISSN - 1098-2345
pISSN - 0275-2565
DOI - 10.1002/ajp.1350130209
Subject(s) - lemur catta , hemoglobin , globin , prosimian , phenotype , biology , lemur , biochemistry , chemistry , genetics , microbiology and biotechnology , primate , gene , ecology
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.