Prosimian hemoglobins I. The primary structure of the βglobin chain of lemur catta

Dorian H. Coppenhaver, James D. Dixon, Lawrence K. Duffy

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

The primary structure of the β chain from the hemoglobin of a prosimian primate, Lemur catta, has been determined by automated Edman degradation of intact polypeptide chain and fragments produced by tryptic, cyanogen bromide and acid cleavage, and by homology with the sequence of Lemur fulvus. The sequence presented here differs from the human βglobin sequence at 26 sites. This is the same degree of divergence previously reported for the βglobin chain of Lemur fulvus. The sequences of the two congeneric lemuroid βglobin chains are surprisingly divergent, differing at 18 sites. Of the 26 positions where L. catta differs from Homo sapiens, 7 are at positions with defined function. Of these 7 positions, 4 (2-Phe, 54-Ile, 94-Val, 112-Ile) are unique to L. catta among the primate βglobin chains of established sequence. Residue 112-Ile is consistent with the prediction of Beard and Goodman (19) of an isoleucyl residue in this position in the ancestral primate βglobin chain.

Original languageEnglish (US)
Pages (from-to)1-14
Number of pages14
JournalHemoglobin
Volume7
Issue number1
DOIs
StatePublished - Jan 1 1983

ASJC Scopus subject areas

  • Hematology
  • Clinical Biochemistry
  • Genetics(clinical)
  • Biochemistry, medical

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