Prosimian hemoglobins-V. The primary structures of the α-I, α-II and β-hemoglobin chains of Hapalemur griseus, with a note on the classification of Microcebus

Lawrence K. Duffy, Joakim Luick, Dorian H. Coppenhaver

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

1. 1. The duplicated adult hemoglobins were isolated from a mature Hapalemur griseus and the constituent chains prepared. Sequence analysis of the isolated α-globins showed that the α-I and α-II chains differed by a glycine for lysine substitution at position 15. 2. 2. The complete amino acid sequence of the single adult β-globin of Hapalemur griseus was determined. The β-globin sequence of Hapalemur griseus clusters with those of other authentic lemurs, and is clearly separated from the sequences characteristic of lorisiform primates. 3. 3. Partial sequence analysis of the β-globin of Microcebus murinus showed only a single amino acid difference when compared to the Hapalemur globin. 4. 4. Partial sequence analysis of the α-globin of Microcebus murinus showed only three amino acid residues that are not found in other lemuriform α-globins; two of these are unique to Microcebus among all known prosimian α-globin sequences. 5. 5. The Microcebus α- and β-globins are more similar to the homologous lemuriform sequences than they are to lorisiform sequences.

Original languageEnglish (US)
Pages (from-to)261-267
Number of pages7
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume97
Issue number2
DOIs
StatePublished - 1990

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology

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