Characterization of bison (Bison bison) myoglobin

Meat Science

Volumn 84, Issue 1, 2010, Pages 71-78

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

^a UNIVERSITY OF KENTUCKY   (United States)

^b UNIVERSITY OF KENTUCKY   (United States)

^c UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

Bison; Edman degradation; Mass spectrometry; Myoglobin; Primary structure; Redox stability; Thermostability

Indexed keywords

4 HYDROPEROXY 2 NONENAL; 4-HYDROPEROXY-2-NONENAL; ALDEHYDE; METMYOGLOBIN; MYOGLOBIN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BUFFALO; CATTLE; CHEMISTRY; COMPARATIVE STUDY; ISOLATION AND PURIFICATION; MASS SPECTROMETRY; MEAT; MOLECULAR GENETICS; MOLECULAR WEIGHT; OXIDATION REDUCTION REACTION; PEPTIDE MAPPING; PH; PIGMENTATION; PROTEIN STABILITY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; TEMPERATURE; TIME;

ALDEHYDES; AMINO ACID SEQUENCE; ANIMALS; BISON; CATTLE; HYDROGEN-ION CONCENTRATION; MEAT; METMYOGLOBIN; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MYOGLOBIN; OXIDATION-REDUCTION; PEPTIDE MAPPING; PIGMENTATION; PROTEIN STABILITY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TEMPERATURE; TIME FACTORS;

BISON; BISON BISON; BOS GRUNNIENS; BOVIDAE; BUBALUS; CAPRA HIRCUS; CERVUS ELAPHUS; OVIS ARIES;

EID: 70349741304     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2009.08.014     Document Type: Article

References (63)

1. Alderton A.L., Faustman C., Liebler D.C., and Hill D.W. Induction of redox instability of bovine myoglobin by adduction with 4-hydroxy-2-nonenal. Biochemistry 42 (2003) 4398-4405
2. Barrick D., Hughson F.M., and Baldwin R.L. Molecular mechanisms of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin. Journal of Molecular Biology 237 (1994) 588-601
3. Brown W.D., and Dolev A. Autoxidation of beef and tuna oxymyoglobins. Journal of Food Science 28 (1963) 207-210
4. Brown W.D., and Mebine L.B. Autoxidation of oxymyoglobin. Journal of Biological Chemistry 244 (1969) 6696-6701
5. Carbone D.L., Doorn J.A., Kiebler Z., and Petersen D.R. Cysteine modification by lipid peroxidation products inhibits protein disulfide isomerase. Chemical Research in Toxicology 18 (2005) 1324-1331
6. Dhanda J.S., Pegg R.B., Janz J.A.M., Aalhus J.L., and Shand P.J. Palatability of bison semimembranosus and effects of marination. Meat Science 62 (2002) 19-26
7. Dosi R., Di Maro A., Chambery A., Colonna G., Costantini S., Geraci G., et al. Characterization and kinetics studies of water-buffalo (Bubalus bubalis) myoglobin. Comparative Biochemistry and Physiology Part B 145 (2006) 230-238
8. Driskell J.A., Marchello M.J., and Giraud D.W. Riboflavin and niacin concentrations of bison cuts. Journal of Animal Science 78 (2000) 1267-1271
9. Driskell J.A., Yuan X., Giraud D.W., Hadley M., and Marchello M.J. Concentrations of selected vitamins and selenium in bison cuts. Journal of Animal Science 75 (1997) 2950-2954
10. D'Souza S.E., Ginsberg M.H., Burke T.A., and 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. Journal of Biological Chemistry 265 (1990) 3440-3446
11. Enoki Y., Matsumura K., Ohga Y., Kohzuki H., and 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 110 (1995) 193-199
12. Esterbauer H., Schaur J.R., and Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radical Biology Medicine 11 (1991) 81-128
13. Faustman C., and Cassens R.G. The biochemical basis for discoloration in fresh meat: A review. Journal of Muscle Foods 1 (1990) 217-243
14. Faustman C., Liebler D.C., McClure T.D., and Sun Q. α, β-Unsaturated aldehydes accelerate oxymyoglobin oxidation. Journal of Agricultural and Food Chemistry 47 (1999) 3140-3144
15. Faustman, C., & Phillips, A. L. (2001). Measurement of discoloration in fresh meat. Ch. F3 Unit F3.3. In Current protocol in food analytical chemistry. New York: Wiley and Sons.
16. Galbraith J.K., Hauer G., Helbig L., Wang Z., Marchello M.J., and Goonewardene L.A. Nutrient profiles in retail cuts of bison meat. Meat Science 74 (2006) 648-654
17. Goto T., and Shikama K. Autoxidation of native oxymyoglobin from bovine heart muscle. Archives of Biochemistry and Biophysics 163 (1974) 476-481
18. Grunwald E.W., and 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 54 (2006) 4452-4460
19. Gu, S., Chen, D., Yin, S., Tang, K., & Sun, Q. (2007). Analysis of cDNA sequence of yak myoglobin and its oxidation in muscles. In Proceedings of 53rd international congress of meat science and technology (pp. 223-224). 5-10 August, 2007, Beijing, China.
20. Gutzke D., and Trout G.R. Temperature and pH dependence of the autoxidation rate of bovine, ovine, porcine, and cervine oxymyoglobin isolated from three different muscles-longissimus dorsi, gluteus medius, and biceps femoris. Journal of Agricultural and Food Chemistry 50 (2002) 2673-2678
21. Han K., Dautrevaux M., Chaila X., and Biserte G. The covalent structure of beef heart myoglobin. European Journal of Biochemistry 16 (1970) 465-471
22. Han K., Tetaert D., Moschetto Y., Dautrevaux M., and Kopeyan C. The covalent structure of sheep-heart myoglobin. European Journal of Biochemistry 27 (1972) 585-592
23. Janz J.A.M., and Aalhus J.L. Meat quality, bacteriology and retail case life of bison Longissimus lumborum following spray chilling. Journal of Muscle Foods 17 (2006) 330-342
24. Janz J.A.M., Aalhus J.L., and Price M.A. Blast chilling and low voltage electrical stimulation influences on bison (Bison bison bison) meat quality. Meat Science 57 (2001) 403-411
25. Janz J.A.M., Aalhus J.L., Price M.A., and Schaefer A.L. The influence of elevated temperature conditioning on bison (Bison bison bison) meat quality. Meat Science 56 (2000) 279-284
26. Joseph, P., Suman, S. P., Li, S., Beach, C. M., & Claus, J. R. (2008). Mass spectrometric characterization and thermostability of turkey myoglobin. In Proceedings of 61st annual reciprocal meat conference, Gainesville, FL. Abstract no. 87.
27. Koch R.M., Jung H.G., Crouse J.D., Varel V.H., and Cundiff L.V. Growth, digestive capability, carcass and meat characteristics of Bison bison, Bos taurus and Bos x Bison. Journal of Animal Science 73 (1995) 1271-1281
28. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T. Nature 227 (1970) 680-685
29. Lee S., Joo S.T., Alderton A.L., Hill D.W., and Faustman C. Oxymyoglobin and lipid oxidation in yellowfin tuna (Thunnus albacares) loins. Journal of Food Science 68 (2003) 1664-1668
30. Lee S., Phillips A.L., Liebler D.C., and Faustman C. Porcine oxymyoglobin and lipid oxidation in vitro. Meat Science 63 (2003) 241-247
31. Manza L.L., Stamer S.L., Ham A.J., Codreanu S.G., and Liebler D.C. Sample preparation and digestion for proteomic analyses using spin filters. Proteomics 5 (2005) 1742-1745
32. Marchello M.J., and Driskell J.A. Nutrient composition of grass and grain finished bison. Great Plains Research 11 (2001) 65-82
33. Marchello M.J., Slanger W.D., Hadley M., Milne D.B., and Driskell J.A. Nutrient composition of bison fed concentrate diets. Journal of Food Composition and Analysis 11 (1998) 231-239
34. Marcinek D.J., Bonaventura J., Wittenberg J.B., and 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 280 (2001) R1123-R1133
35. National Bison Association. (2009). .
36. Pietrasik Z., Dhanda J.S., Pegg R.B., and Shand P.J. The effects of marination and cooking regimes in the water-binding properties and tenderness of beef and bison top round roasts. Journal of Food Science 70 (2005) S102-S106
37. Pietrasik Z., Dhanda J.S., Shand P.J., and Pegg R.B. Influence of injection, packaging, and storage conditions on the quality of beef and bison steaks. Journal of Food Science 71 (2006) S110-S118
38. Ponce-Alquicira E., and Taylor A.J. Extraction and ESI-CID-MS/MS analysis of myoglobins from different meat species. Food Chemistry 69 (2000) 81-86
39. Ramanathan R., Konda M.K.R., Mancini R.A., and Faustman C. Species-specific effects of sarcoplasmic extracts on lipid oxidation in vitro. Journal of Food Science 74 (2009) C73-C76
40. Regis W.C.B., Fattori J., Santoro M.M., Jamin M., and Ramos C.H.I. On the difference in stability between horse and sperm whale myoglobins. Archives of Biochemistry and Biophysics 436 (2005) 168-177
41. Rosenfeld J., Capdevielle J., Guillemot J.C., and Ferrara P. In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis. Analytical Biochemistry 203 (1992) 173-179
42. Rousseaux J., Dautrevaux M., and Han K. Comparison of the amino acid sequence of pig heart myoglobin with other ungulate myoglobin. Biochimica et Biophysica Acta 439 (1976) 55-62
43. Rule D.C., Broughton K.S., Shellito S.M., and Maiorano G. Comparison of muscle fatty acid profiles and cholesterol concentrations of bison, beef cattle, elk and chicken. Journal of Animal Science 80 (2002) 1202-1211
44. Sakai T., Kuwazuru S., Yamauchi K., and Uchida K. A lipid peroxidation-derived aldehyde, 4-hydroxy-2-nonenal and w-6-fatty acids contents in meats. Bioscience, Biotechnology, and Biochemistry 59 (1995) 1379-1380
45. Sakai T., Yamauchi K., Kuwazuru S., and Gotoh N. Relationships between 4-hydroxy-2-nonenal, 2-thiobarbituric acid reactive substances and n-6 polyunsaturated fatty acids in refrigerated and frozen pork. Bioscience, Biotechnology, and Biochemistry 62 (1998) 2028-2029
46. SAS. (2007). SAS System for Windows: Release 9.1, SAS Institute Inc., Cary, NC, USA.
47. Schneider C., Tallman K.A., Porter N.A., and Brash A.R. Two distinct pathways of formation of 4-hydroxynonenal. Journal of Biological Chemistry 276 (2001) 20831-20838
48. Stewart J.M., Blakely J.A., Karpowicz P.A., Kalanxhi E., Thatcher B.J., and 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 137 (2004) 401-412
49. Suman S.P., Faustman C., Stamer S.L., and 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 54 (2006) 3402-3408
50. Suman S.P., Faustman C., Stamer S.L., and Liebler D.C. Proteomics of lipid oxidation-induced oxidation in porcine and bovine oxymyoglobins. Proteomics 7 (2007) 628-640
51. Suman S.P., Joseph P., Li S., Steinke L., and Fontaine M. Primary structure of goat myoglobin. Meat Science 82 (2009) 456-460
52. Suman S.P., Mancini R.A., and Faustman C. Lipid-oxidation-induced carboxymyoglobin oxidation. Journal of Agricultural and Food Chemistry 54 (2006) 9248-9253
53. Tada T., Watanabe Y.H., Matsuoka A., Ikeda-Saito M., Imai K., Ni-hei Y., et al. African elephant myoglobin with an unusual autoxidation behavior: Comparison with the H64Q mutant of sperm whale myoglobin. Biochimica et Biophysica Acta 1387 (1998) 165-176
54. Tang J., Faustman C., and Hoagland T.A. Krzywicki revisited: Equations for spectrophotometric determination of myoglobin redox forms in aqueous meat extracts. Journal of Food Science 69 (2004) C717-720
55. Trout G.R. Variation in myoglobin denaturation and color of cooked beef, pork, and turkey meat as influenced by pH, sodium chloride, sodium tripolyphosphate, and cooking temperature. Journal of Food Science 54 (1989) 536-544
56. Ueki N., Chow C.J., and Ochiai Y. Characterization of bullet tuna myoglobin with reference to thermostability-structure relationship. Journal of Agricultural and Food Chemistry 53 (2005) 4968-4975
57. Ueki N., and Ochiai Y. Primary structure and thermostability of bigeye tuna myoglobin in relation to those from other scombridae fish. Fisheries Science 70 (2004) 875-884
58. Ueki N., and Ochiai Y. Effect of amino acid replacements on the structural stability of fish myoglobin. Journal of Biochemistry 140 (2006) 649-656
59. USDA. (1997). USDA advises consumers to use a meat thermometer when cooking hamburger. FSIS News and Information Bulletin. FSIS, USDA. Washington, DC.
60. USDA. (2003). USDA FSIS Fact sheets. .
61. Wood J.D., Enser M., Fisher A.V., Nute G.R., Richardson R.I., and Sheard P.R. Manipulating meat quality and composition. Proceedings of the Nutrition Society 58 (1999) 363-370
62. Ye J., McGinnis S., and Madden T.L. BLAST: Improvements for better sequence analysis. Nucleic Acids Research 34 (2006) W6-W9
63. Yuan X., Marchello M.J., and Driskell J.A. Selected vitamin contents and retentions in bison patties as related to cooking method. Journal of Food Science 64 (1999) 462-464