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

✍ Scribed by Lawrence K. Duffy; Margaret M. Ehrhardt; John Buettner-Janusch; Dorian H. Coppenhaver

Publisher: John Wiley and Sons
Year: 1987
Tongue: English
Weight: 405 KB
Volume: 13
Category: Article
ISSN: 0275-2565
DOI: 10.1002/ajp.1350130209

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✦ Synopsis

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 a-globins was observed at position 15 (a I-Gly, a 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 (a I-Gly, a 11-Ala). The complete primary structures of the duplicated a-globin chains of Lemur catta are presented.

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