Primary structure of goat myoglobin

S. P. Suman, P. Joseph, S. Li, L. Steinke, M. Fontaine

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


Color stability attributes of goat meat are different from those of sheep meat, possibly due to species-specific differences in myoglobin (Mb) biochemistry. An examination of post-genomic era protein databases revealed that the primary structure of goat Mb has not been determined. Therefore, our objective was to characterize the primary structure of goat Mb. Goat Mb was isolated from cardiac muscles employing ammonium sulfate precipitation and gel-filtration chromatography, and Edman degradation was utilized to determine the amino acid sequence. Sequence analyses of intact Mb as well as tryptic- and cyanogen bromide-peptides yielded the complete primary structure of goat Mb, which shared 98.7% similarity with sheep Mb. Similar to other livestock myoglobins goat Mb has 153 residues. Comparison of the sequences of goat and sheep myoglobins revealed two amino acid substitutions - THRgoat8GLNsheep and GLYgoat52GLUsheep. Goat Mb contains 12 histidine residues. As observed in other meat-producing livestock species, distal and proximal histidines, responsible for stabilizing the heme group and coordinating oxygen-binding, are conserved in goat Mb.

Original languageEnglish
Pages (from-to)456-460
Number of pages5
JournalMeat Science
Issue number4
StatePublished - Aug 2009

Bibliographical note

Funding Information:
This work was supported by funds from the Kentucky Agricultural Experiment Station, University of Kentucky.

Copyright 2011 Elsevier B.V., All rights reserved.


  • Capra hircus
  • Edman degradation
  • Goat meat
  • Mass spectrometry
  • Meat color
  • Myoglobin
  • Primary structure

ASJC Scopus subject areas

  • Food Science


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