title: Amino acid sequence of myoglobin from white-tailed deer (Odocoileus virginianus).
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.
authors.affiliation: Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, USA.
authors.forename: Poulson
authors.initials: P
authors.lastname: Joseph
authors.forename: Surendranath P
authors.initials: SP
authors.lastname: Suman
authors.forename: Shuting
authors.initials: S
authors.lastname: Li
authors.forename: Michele
authors.initials: M
authors.lastname: Fontaine
authors.forename: Laurey
authors.initials: L
authors.lastname: Steinke
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D003670:Deer; D004044:Dietary Proteins / Q000032:analysis*; D006418:Heme / Q000032:analysis; D006639:Histidine / Q000032:analysis; D008460:Meat / Q000032:analysis*; D008969:Molecular Sequence Data; D009206:Myocardium / Q000737:chemistry*; D009211:Myoglobin / Q000737:chemistry*; D012418:Ruminants; D020539:Sequence Analysis, Protein / Q000379:methods
chemical_list: D000596:Amino Acids; D004044:Dietary Proteins; D009211:Myoglobin; D006418:Heme; D006639:Histidine