Primary structure of goat myoglobin

Meat Science

Volumn 82, Issue 4, 2009, Pages 456-460

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

^a UNIVERSITY OF KENTUCKY   (United States)

^b UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

Capra hircus; Edman degradation; Goat meat; Mass spectrometry; Meat color; Myoglobin; Primary structure

Indexed keywords

CAPRA HIRCUS; OVIS ARIES;

EID: 67349117661     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2009.02.017     Document Type: Article

References (48)

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. Alexandre G., and Mandonnet N. Goat meat production in harsh environments. Small Ruminant Research 60 (2005) 53-66
3. Babiker S.A., El Khider I.A., and Shafie S.A. Chemical composition and quality attributes of goat meat and lamb. Meat Science 28 (1990) 273-277
4. Brantley Jr. R.E., Smerdon S.J., Wilkinson A.J., Singleton E.W., and Olson J.S. The mechanism of autoxidation of myoglobin. Journal of Biological Chemistry 268 (1993) 6995-7010
5. Brown W.D., and Dolev A. Autoxidation of beef and tuna oxymyoglobins. Journal of Food Science 28 (1963) 207-210
6. Brown W.D., and Mebine L.B. Autoxidation of oxymyoglobin. Journal of Biological Chemistry 244 (1969) 6696-6701
7. 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
8. Dautrevaux M., Boulanger Y., Han K., and Biserte G. Covalent structure of horse myoglobin. European Journal of Biochemistry 11 (1969) 267-277
9. Dene H., Goodman M., and Romero-Herrera A.E. The amino acid sequence of elephant (Elephas maximus) myoglobin and the phylogeny of Proboscidea. Proceedings of the Royal Society of London, Series B, Biological Sciences B207 (1980) 111-127
10. 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
11. 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
12. 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
13. Fang J., and Holmgren A. Inhibition of thioredoxin and thioredoxin reductase by 4-hydroxy-2-nonenal in vitro and in vivo. Journal of the American Chemical Society 128 (2006) 1879-1885
14. FAO. (2008). .
15. Faustman C., and Phillips A.L. Measurement of discoloration in fresh meat. Ch. F3 Unit F3.3. In current protocol in food analytical chemistry (2001), Wiley and Sons, New York
16. Giardina B., Ascenzi P., Clementi M.E., De Sanctisi D., Rizzi M., and Colettai M. Functional modulation by lactate of myoglobin. A monomeric allosteric hemoprotein. Journal of Biological Chemistry 271 (1996) 16999-17001
17. Glimp H.A. Meat goat production and marketing. Journal of Animal Science 73 (1995) 291-295
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. 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
20. Han K., Dautrevaux M., Chaila X., and Biserte G. The covalent structure of beef heart myoglobin. European Journal of Biochemistry 16 (1970) 465-471
21. 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
22. Kadim I.T., Mahgoub O., Al-Ajmi D.S., Al-Maqbaly R.S., Al-Saqri N.M., and Ritchie A. An evaluation of the growth, carcass and meat quality characteristics of Omani goat breeds. Meat Science 66 (2003) 203-210
23. Kadim I.T., Mahgoub O., Al-Marzooqi W., Al-Ajmi D.S., Al-Maqbali R.S., and Al-Lawati S.M. The influence of seasonal temperatures on meat quality characteristics of hot-boned, m. psoas major and minor, from goats and sheep. Meat Science 80 (2008) 210-215
24. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T. Nature 227 (1970) 680-685
25. Lee J.H., Kannan G., Eega K.R., Kouakou B., and Getz W.R. Nutritional and quality characteristics of meat from goats and lambs finished under identical dietary regime. Small Ruminant Research 74 (2008) 255-259
26. Livingston D.J., and Brown W.D. The chemistry of myoglobin and its reaction. Food Technology 35 (1981) 244-252
27. Mancini R.A., and Ramanathan R. Sodium lactate influences myoglobin redox stability in vitro. Meat Science 78 (2008) 529-532
28. 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
29. 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
30. 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
31. Romero-Herrera A.E., Goodman M., Dene H., Bartnicki D.E., and Mizukami H. An exceptional amino acid replacement on the distal side of the iron atom in Proboscidean myoglobin. Journal of Molecular Evolution 17 (1981) 140-147
32. 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
33. 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
34. Schonfeldt H.C., Naude R.T., Bok W., van Heerden S.M., Smit R., and Boshoff E. Flavour and tenderness related quality characteristics of goat and sheep meat. Meat Science 34 (1993) 363-379
35. Sen A.R., Santra A., and Karim S.A. Carcass yield, composition and meat quality attributes of sheep and goat under semiarid conditions. Meat Science 66 (2004) 757-763
36. Sheridan R., Hoffman L.C., and Ferreira A.V. Meat quality of Boer goat kids and mutton Merino lambs. 2. Sensory meat evaluation. Animal Science 76 (2003) 73-79
37. Shrestha J.N.B., and Fahmy M.H. Breeding goats for meat production: A review. 1. Genetic resources, management and breed evaluation. Small Ruminant Research 58 (2005) 93-106
38. Simela L., and Merkel R. The contribution of chevon from Africa to global meat production. Meat Science 80 (2008) 101-109
39. 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
40. 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
41. 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 2006 54 (2006) 3402-3408
42. 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
43. Tamburrini M., Romano M., Giardina B., and 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 122 (1999) 235-240
44. Tshabalala P.A., Strydom P.E., Webb E.C., and de Kock H.L. Meat quality of designated South African indigenous goat and sheep breeds. Meat Science 65 (2003) 563-570
45. Ueki N., and Ochiai Y. Effect of amino acid replacements on the structural stability of fish myoglobin. Journal of Biochemistry 140 (2006) 649-656
46. 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
47. Webb E.C., Casey N.H., and Simela L. Goat meat quality. Small Ruminant Research 60 (2005) 153-166
48. Ye J., McGinnis S., and Madden T.L. BLAST: Improvements for better sequence analysis. Nucleic Acids Research 34 (2006) W6-W9