Amino acid sequence of myoglobin from emu (Dromaius novaehollandiae) skeletal muscle

S. P. Suman, P. Joseph, S. Li, C. M. Beach, M. Fontaine, Laurey A Steinke

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

The objective of the present study was to characterize the primary structure of emu myoglobin (Mb). Emu Mb was isolated from Iliofibularis muscle employing gel-filtration chromatography. Matrix Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry was employed to determine the exact molecular mass of emu Mb in comparison with horse Mb, and Edman degradation was utilized to characterize the amino acid sequence. The molecular mass of emu Mb was 17,380. Da and was close to those reported for ratite and poultry myoglobins. Similar to myoglobins from meat-producing livestock and birds, emu Mb has 153 amino acids. Emu Mb contains 9 histidines. Proximal and distal histidines, responsible for coordinating oxygen-binding property of Mb, are conserved in emu. Emu Mb shared more than 90% homology with ratite and chicken myoglobins, whereas it demonstrated only less than 70% sequence similarity with ruminant myoglobins.

Original languageEnglish (US)
Pages (from-to)623-628
Number of pages6
JournalMeat Science
Volume86
Issue number3
DOIs
Publication statusPublished - Nov 1 2010

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Keywords

  • Dromaius novaehollandiae
  • Edman degradation
  • Emu
  • Mass spectrometry
  • Myoglobin
  • Primary structure

ASJC Scopus subject areas

  • Food Science

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