Amino acid sequence of myoglobin from emu (Dromaius novaehollandiae) skeletal muscle
| Autor: | Surendranath P. Suman, Laurey Steinke, S. Li, C.M. Beach, P. Joseph, Michele Fontaine |
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| Rok vydání: | 2010 |
| Předmět: |
Livestock
Molecular Sequence Data Muscle Proteins Palaeognathae Mass Spectrometry chemistry.chemical_compound immune system diseases hemic and lymphatic diseases Animals Histidine Amino Acid Sequence Horses Muscle Skeletal Peptide sequence chemistry.chemical_classification Dromaiidae Sequence Homology Amino Acid biology Molecular mass Edman degradation Myoglobin symbols.heraldic_supporter Protein primary structure Ruminants biology.organism_classification Amino acid Molecular Weight chemistry Biochemistry Chromatography Gel symbols Dromaius novaehollandiae Chickens Ratite Food Science |
| Zdroj: | Meat Science. 86:623-628 |
| ISSN: | 0309-1740 |
| DOI: | 10.1016/j.meatsci.2010.04.041 |
| Popis: | The objective of the present study was to characterize the primary structure of emu myoglobin (Mb). Emu Mb was isolated from Iliofibularis muscle employing gel-filtration chromatography. Matrix Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry was employed to determine the exact molecular mass of emu Mb in comparison with horse Mb, and Edman degradation was utilized to characterize the amino acid sequence. The molecular mass of emu Mb was 17,380 Da and was close to those reported for ratite and poultry myoglobins. Similar to myoglobins from meat-producing livestock and birds, emu Mb has 153 amino acids. Emu Mb contains 9 histidines. Proximal and distal histidines, responsible for coordinating oxygen-binding property of Mb, are conserved in emu. Emu Mb shared more than 90% homology with ratite and chicken myoglobins, whereas it demonstrated only less than 70% sequence similarity with ruminant myoglobins. |
| Databáze: | OpenAIRE |
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