Amino acid sequence of myoglobin from white-tailed deer (Odocoileus virginianus)
| Autor: | P. Joseph, Laurey Steinke, S. Li, Michele Fontaine, Surendranath P. Suman |
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| Rok vydání: | 2012 |
| Předmět: |
Meat
animal diseases Molecular Sequence Data Heme Biology Odocoileus chemistry.chemical_compound Sequence Analysis Protein parasitic diseases Animals Histidine Amino Acid Sequence Amino Acids Peptide sequence Ammonium sulfate precipitation chemistry.chemical_classification Edman degradation Myoglobin Deer Myocardium Protein primary structure Ruminants biology.organism_classification Amino acid chemistry Biochemistry Dietary Proteins Food Science |
| Zdroj: | Meat Science. 92:160-163 |
| ISSN: | 0309-1740 |
| DOI: | 10.1016/j.meatsci.2012.04.012 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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