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

作者：Joseph Poulson; Suman Surendranath P^*; Li Shuting; Fontaine Michele; Steinke Laurey

来源：Meat Science, 2012, 92(2): 160-163.

DOI：10.1016/j.meatsci.2012.04.012

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

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.

• 出版日期2012-10