Amino acid sequence of myoglobin from white-tailed deer (Odocoileus virginianus)

Poulson Joseph, Surendranath P. Suman, Shuting Li, Michele Fontaine, Laurey Steinke

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Our objective was to determine the primary structure of white-tailed deer myoglobin (Mb). White-tailed deer Mb was isolated from cardiac muscles employing ammonium sulfate precipitation and gel-filtration chromatography. The amino acid sequence was determined by Edman degradation. Sequence analyses of intact Mb as well as tryptic- and cyanogen bromide-peptides yielded the complete primary structure of white-tailed deer Mb, which shared 100% similarity with red deer Mb. White-tailed deer Mb consists of 153 amino acid residues and shares more than 96% sequence similarity with myoglobins from meat-producing ruminants, such as cattle, buffalo, sheep, and goat. Similar to sheep and goat myoglobins, white-tailed deer Mb contains 12 histidine residues. Proximal (position 93) and distal (position 64) histidine residues responsible for maintaining the stability of heme are conserved in white-tailed deer Mb.

Original languageEnglish
Pages (from-to)160-163
Number of pages4
JournalMeat Science
Issue number2
StatePublished - Oct 2012

Bibliographical note

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


  • Edman degradation
  • Myoglobin
  • Odocoileus virginianus
  • Primary structure
  • White-tailed deer

ASJC Scopus subject areas

  • Food Science


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