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.
Original language | English (US) |
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Pages (from-to) | 160-163 |
Number of pages | 4 |
Journal | Meat Science |
Volume | 92 |
Issue number | 2 |
DOIs | |
State | Published - Oct 2012 |
Keywords
- Edman degradation
- Myoglobin
- Odocoileus virginianus
- Primary structure
- White-tailed deer
ASJC Scopus subject areas
- Food Science