Amino acid sequence of myoglobin from emu (Dromaius novaehollandiae) skeletal muscle

Meat Science

Volumn 86, Issue 3, 2010, Pages 623-628

  Suman, S P ^a   Joseph, P ^a   Li, S ^a   Beach, C M ^b   Fontaine, M ^c   Steinke, L ^c  

^a UNIVERSITY OF KENTUCKY   (United States)

^b UNIVERSITY OF KENTUCKY   (United States)

^c UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

Dromaius novaehollandiae; Edman degradation; Emu; Mass spectrometry; Myoglobin; Primary structure

Indexed keywords

DROMAIUS NOVAEHOLLANDIAE; EDMAN DEGRADATION; EMU; MYOGLOBIN; PRIMARY STRUCTURE;

AGRICULTURE; AMINO ACIDS; BINDING ENERGY; BIRDS; DEGRADATION; DESORPTION; DRUG PRODUCTS; MASS SPECTROMETRY; MOLECULAR MASS; MUSCLE; OXYGEN;

POULTRY;

HISTIDINE; MUSCLE PROTEIN; MYOGLOBIN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BIRD; BOVIDS; CHEMISTRY; CHICKEN; GEL CHROMATOGRAPHY; HORSE; ISOLATION AND PURIFICATION; LIVESTOCK; MASS SPECTROMETRY; MOLECULAR GENETICS; MOLECULAR WEIGHT; SEQUENCE HOMOLOGY; SKELETAL MUSCLE;

AMINO ACID SEQUENCE; ANIMALS; CHICKENS; CHROMATOGRAPHY, GEL; DROMAIIDAE; HISTIDINE; HORSES; LIVESTOCK; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUSCLE PROTEINS; MUSCLE, SKELETAL; MYOGLOBIN; PALAEOGNATHAE; RUMINANTS; SEQUENCE HOMOLOGY, AMINO ACID;

AVES; BOVIDAE; DROMAIUS NOVAEHOLLANDIAE; EQUIDAE; PALAEOGNATHAE;

EID: 79958150387     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2010.04.041     Document Type: Article

References (51)

1. American Emu Association. (2009) http://www.aea-emu.org.
2. Andrews L., Gillespie J., Schupp A. Ratite meat sensory scores compared with beef. Journal of Food Quality 2000, 23:351-359.
3. Beckerbauer L.M., Thiel-Cooper R., Ahn D.U., Sell J.L., Parrish F.C., Beitz D.C. Influence of two dietary fats on the composition of emu oil and meat. Poultry Science 2001, 80:187-194.
4. Berge P., Lepetit J., Renerre M., Touraille C. Meat quality traits in the emu (Dromaius novaehollandiae) as affected by muscle type and animal age. Meat Science 1997, 45:209-221.
5. Brown W.D., Mebine L.B. Autoxidation of oxymyoglobin. The Journal of Biological Chemistry 1969, 244:6696-6701.
6. Daniel D.R., Thompson L.D., Hoover L.C. Nutrition composition of emu compares favorably with that of other lean meats. Journal of the American Dietetic Association 2000, 100:836-838.
7. Dautrevaux M., Boulanger Y., Han K., Biserte G. Covalent structure of horse myoglobin. European Journal of Biochemistry 1969, 11:267-277.
8. Deconinck M., Peiffer S., Depreter J., Paul C., Schnek A.G., Leonis J. The primary sequence of chicken myoglobin (Gallus gallus). Biochimica et Biophysica Acta 1975, 386:567-575.
9. Dosi R., Di Maro A., Chambery A., Colonna G., Costantini S., Geraci G., Parente A. Characterization and kinetics studies of water buffalo (Bubalus bubalis) myoglobin. Comparative Biochemistry and Physiology Part B 2006, 145:230-238.
10. D'Souza S.E., Ginsberg M.H., Burke T.A., Plow E.F. The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its alpha subunit. The Journal of Biological Chemistry 1990, 265:3440-3446.
11. Enoki Y., Matsumura K., Ohga Y., Kohzuki H., Hattori M. Oxygen affinities (P50) of myoglobins from four vertebrate species (Canis familiaris, Rattus norvegicus, Mus musculus and Gallus domesticus) as determined by a kinetic and an equilibrium method. Comparative Biochemistry and Physiology Part B 1995, 110:193-199.
12. Enoki Y., Ohga Y., Ishidate H., Morimoto T. Primary structure of myoglobin from 31 species of birds. Comparative Biochemistry and Physiology, Part B 2008, 149:11-21.
13. Fang J., Holmgren A. Inhibition of thioredoxin and thioredoxin reductase by 4-hydroxy-2-nonenal in vitro and in vivo. Journal of the American Chemical Society 2006, 128:1879-1885.
14. Faustman C., Liebler D.C., McClure T.D., Sun Q. α, ß-Unsaturated aldehydes accelerate oxymyoglobin oxidation. Journal of Agricultural and Food Chemistry 1999, 47:3140-3144.
15. Faustman C., Phillips A.L. Measurement of discoloration in fresh meat. Ch. F3 Unit F3.3. Current Protocol in Food Analytical Chemistry 2001, Wiley and Sons, New York.
16. Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., Bairoch A. Protein identification and analysis tools on the ExPASy Server. The proteomics protocols handbook 2005, 571-607. Humana Press, Totowa. J.M. Walker (Ed.).
17. Giardina B., Ascenzi P., Clementi M.E., De Sanctisi D., Rizzi M., Colettai M. Functional modulation by lactate of myoglobin. A monomeric allosteric hemoprotein. Journal of Biological Chemistry 1996, 271:16999-17001.
18. Gillespie J.M., Schupp A.R. Ratite production as an agricultural enterprise. The Veterinary Clinics of North America. Food Animal Practice 1998, 14:373-386.
19. Grunwald E.W., Richards M.P. Studies with myoglobin variants indicate that released hemin is the primary promoter of lipid oxidation in washed fish muscle. Journal of Agricultural and Food Chemistry 2006, 54:4452-4460.
20. Han K., Dautrevaux M., Chaila X., Biserte G. The covalent structure of beef heart myoglobin. European Journal of Biochemistry 1970, 16:465-471.
21. Han K., Tetaert D., Moschetto Y., Dautrevaux M., Kopeyan C. The covalent structure of sheep-heart myoglobin. European Journal of Biochemistry 1972, 27:585-592.
22. Hoffman L.C. A review of the research conducted on ostrich meat. Proceedings of the 3rd international ratite scientific symposium and XII world ostrich congress 2005, 107-119. World's Poultry Science Association, Savoy, IL.
23. Hoffman L.C. The yield and nutritional value of meat from African ungulates, camelidae, rodents, ratites and reptiles. Meat Science 2008, 80:94-100.
24. Hoffman L.C. Value adding and processing of ratite meat: A review. Australian Journal of Experimental Agriculture 2008, 48:1270-1275.
25. Hoffman L.C., Wiklund E. Game and venison-meat for the modern consumer. Meat Science 2006, 74:197-208.
26. Joseph P., Suman S.P., Li S., Beach C.M., Claus J.R. Mass spectrometric characterization and thermostability of turkey myoglobin. LWT Food Science and Technology 2010, 43:273-278.
27. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T. Nature 1970, 227:680-685.
28. Livingston D.J., Brown W.D. The chemistry of myoglobin and its reaction. Food Technology 1981, 35:244-252.
29. Manza L.L., Stamer S.L., Ham A.J., Codreanu S.G., Liebler D.C. Sample preparation and digestion for proteomic analyses using spin filters. Proteomics 2005, 5:1742-1745.
30. Marcinek D.J., Bonaventura J., Wittenberg J.B., Block B.A. Oxygen affinity and amino acid sequence of myoglobins from endothermic and ectothermic fish. American Journal of Physiology: Regulatory, Integrative and Comparative Physiology 2001, 280:R1123-R1133.
31. Pegg R.B., Amarowicz R., Code W.E. Nutritional characteristics of emu (Dromaius novaehollandiae) meat and its value-added products. Food Chemistry 2006, 97:193-202.
32. Ponce-Alquicira E., Taylor A.J. Extraction and ESI-CID-MS/MS analysis of myoglobins from different meat species. Food Chemistry 2000, 69:81-86.
33. Regis W.C.B., Fattori J., Santoro M.M., Jamin M., Ramos C.H.I. On the difference in stability between horse and sperm whale myoglobins. Archives of Biochemistry and Biophysics 2005, 436:168-177.
34. Rosenfeld J., Capdevielle J., Guillemot J.C., Ferrara P. In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis. Analytical Biochemistry 1992, 203:173-179.
35. Rousseaux J., Dautrevaux M., Han K. Comparison of the amino acid sequence of pig heart myoglobin with other ungulate myoglobin. Biochimica et Biophysica Acta 1976, 439:55-62.
36. Saadoun A., Cabrera M.C. A review of the nutritional content and technological parameters of indigenous sources of meat in South America. Meat Science 2008, 80:570-581.
37. Sales J. The emu (Dromaius novaehollandiae): A review of its biology and commercial products. Avian and Poultry Biology Reviews 2007, 18:1-20.
38. Sales J., Horbanczuk J. Ratite meat. World's Poultry Science Journal 1998, 54:59-67.
39. Stewart J.M., Blakely J.A., Karpowicz P.A., Kalanxhi E., Thatcher B.J., Martin B.M. Unusually weak oxygen binding, physical properties, partial sequence, autoxidation rate and a potential phosphorylation site of beluga whale (Delphinapterus leucas) myoglobin. Comparative Biochemistry and Physiology Part B 2004, 137:401-412.
40. Suman S.P., Faustman C., Stamer S.L., Liebler D.C. Redox instability induced by 4-hydroxy-2-nonenal in porcine and bovine myoglobins at pH 5.6 and 4°C. Journal of Agricultural and Food Chemistry 2006, 54:3402-3408.
41. Suman S.P., Faustman C., Stamer S.L., Liebler D.C. Proteomics of lipid oxidation-induced oxidation in porcine and bovine oxymyoglobins. Proteomics 2007, 7:628-640.
42. Suman S.P., Joseph P., Li S., Steinke L., Fontaine M. Primary structure of goat myoglobin. Meat Science 2009, 82:456-460.
43. Tada T., Watanabe Y.H., Matsuoka A., Ikeda-Saito M., Imai K., Ni-Hei Y., Shikama K. African elephant myoglobin with an unusual autoxidation behavior: Comparison with the H64Q mutant of sperm whale myoglobin. Biochimica et Biophysica Acta 1998, 1387:165-176.
44. Tamburrini M., Romano M., Giardina B., Di Prisco G. The myoglobin of Emperor penguin (Aptenodytes forsteri): Amino acid sequence and functional adaptation to extreme conditions. Comparative Biochemistry and Physiology Part B 1999, 122:235-240.
45. Taylor A.J., Linforth R., Weir O., Hutton T., Green B. Potential of electrospray mass spectrometry for meat pigment identification. Meat Science 1993, 33:75-83.
46. Ueki N., Chow C.J., Ochiai Y. Characterization of bullet tuna myoglobin with reference to thermostability-structure relationship. Journal of Agricultural and Food Chemistry 2005, 53:4968-4975.
47. Ueki N., Ochiai Y. Effect of amino acid replacements on the structural stability of fish myoglobin. Journal of Biochemistry 2006, 140:649-656.
48. Votsch W., Anderer F.A. The amino acid sequence of myoglobin from skeletal muscles of red deer (Cervus elaphus). Journal of Molecular Evolution 1975, 5:315-326.
49. Wang Y.W., Sunwoo H., Sim J.S., Cherian G. Lipid characteristics of emu meat and tissues. Journal of Food Lipids 2000, 7:71-82.
50. Wittenberg J.B., Wittenberg B.A. Myoglobin function reassessed. The Journal of Experimental Biology 2003, 206:2011-2020.
51. Ye J., McGinnis S., Madden T.L. BLAST: Improvements for better sequence analysis. Nucleic Acids Research 2006, 34:W6-W9.