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Updated: May 22, 2026

An Integrated Approach for Microprotein Identification and Sequence Analysis
Published on: July 12, 2022
Amino acid sequence of myoglobin from white-tailed deer (Odocoileus virginianus)
Poulson Joseph1, Surendranath P Suman, Shuting Li
1Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, USA.
Abstract:
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.
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