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Volumn 129, Issue 1, 2011, Pages 175-178

Primary structure of turkey myoglobin

Author keywords

Edman degradation; Meleagris gallopavo; Myoglobin; Primary structure; Turkey

Indexed keywords

EDMAN DEGRADATION; MELEAGRIS GALLOPAVO; MYOGLOBIN; PRIMARY STRUCTURES; TURKEY;

EID: 79958169701     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2011.04.024     Document Type: Article
Times cited : (15)

References (30)
  • 3
    • 0015997922 scopus 로고
    • Isolation and purification of turkey heme proteins
    • Cornish, D. G., & Froning, G. W. (1974). Isolation and purification of turkey heme proteins. Poultry Science, 53, 365-377.
    • (1974) Poultry Science , vol.53 , pp. 365-377
    • Cornish, D.G.1    Froning, G.W.2
  • 6
    • 0000369624 scopus 로고
    • A method for the determination of amino acid sequence in peptides
    • Edman, P. (1949). A method for the determination of amino acid sequence in peptides. Archives of Biochemistry, 22, 475.
    • (1949) Archives of Biochemistry , vol.22 , pp. 475
    • Edman, P.1
  • 8
    • 0037392859 scopus 로고    scopus 로고
    • Pink color defect in poultry white meat as affected by endogenous conditions
    • Holownia, K., Chinnan, M. S., & Reynolds, A. E. (2003). Pink color defect in poultry white meat as affected by endogenous conditions. Journal of Food Science, 68, 742-747. (Pubitemid 36453464)
    • (2003) Journal of Food Science , vol.68 , Issue.3 , pp. 742-747
    • Holownia, K.1    Chinnan, M.S.2    Reynolds, A.E.3
  • 9
    • 1942473835 scopus 로고    scopus 로고
    • Cooked chicken breast meat conditions related to simulated pink defect
    • Holownia, K., Chinnan, M. S., & Reynolds, A. E. (2004). Cooked chicken breast meat conditions related to simulated pink defect. Journal of Food Science, 69, C194-C199.
    • (2004) Journal of Food Science , vol.69
    • Holownia, K.1    Chinnan, M.S.2    Reynolds, A.E.3
  • 10
    • 0042207454 scopus 로고    scopus 로고
    • Evaluation of induced color changes in chicken breast meat during simulation of pink color defect
    • Holownia, K., Chinnan, M. S., Reynolds, A. E., & Koehler, P. E. (2003). Evaluation of induced color changes in chicken breast meat during simulation of pink color defect. Poultry Science, 82, 1049-1059. (Pubitemid 38641922)
    • (2003) Poultry Science , vol.82 , Issue.6 , pp. 1049-1059
    • Holownia, K.1    Chinnan, M.S.2    Reynolds, A.E.3    Koehler, P.E.4
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 70350565573 scopus 로고    scopus 로고
    • Washington, DC: American Meat Institute
    • Nalivka, J. (2003). Meat and poultry facts. Washington, DC: American Meat Institute.
    • (2003) Meat and Poultry Facts
    • Nalivka, J.1
  • 16
    • 0036133819 scopus 로고    scopus 로고
    • Carbon monoxide-heme pigment is responsible for the pink color in irradiated raw turkey breast meat
    • Nam, K. C., & Ahn, D. U. (2002). Carbon monoxide-heme pigment is responsible for the pink color in irradiated raw turkey breast meat. Meat Science, 60, 25-33.
    • (2002) Meat Science , vol.60 , pp. 25-33
    • Nam, K.C.1    Ahn, D.U.2
  • 17
    • 79958141122 scopus 로고    scopus 로고
    • National Turkey Federation
    • National Turkey Federation (2007). 〈http://www.eatturkey.com〉.
    • (2007)
  • 18
    • 77951666612 scopus 로고    scopus 로고
    • Detection of 4-hydroxy-2-nonenal adducts of turkey and chicken myoglobins using mass spectrometry
    • Naveena, B. M., Faustman, C., Tatiyaborworntham, N., Yin, S., Ramanathan, R., & Mancini, R. A. (2010). Detection of 4-hydroxy-2-nonenal adducts of turkey and chicken myoglobins using mass spectrometry. Food Chemistry, 122, 836-840.
    • (2010) Food Chemistry , vol.122 , pp. 836-840
    • Naveena, B.M.1    Faustman, C.2    Tatiyaborworntham, N.3    Yin, S.4    Ramanathan, R.5    Mancini, R.A.6
  • 19
    • 0015776538 scopus 로고
    • Automated Edman degradation: The protein sequenator
    • Niall, H. D. (1973). Automated Edman degradation: The protein sequenator. Methods in Enzymology, 27, 942-1010.
    • (1973) Methods in Enzymology , vol.27 , pp. 942-1010
    • Niall, H.D.1
  • 20
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis
    • Rosenfeld, J., Capdevielle, J., Guillemot, J. C., & Ferrara, P. (1992). In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis. Analytical Biochemistry, 203, 173-179.
    • (1992) Analytical Biochemistry , vol.203 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 21
    • 0037391085 scopus 로고    scopus 로고
    • Citric acid and sodium citrate effects on reducing pink color defect of cooked intact turkey breasts and ground turkey rolls
    • Sammel, L. M., & Claus, J. R. (2003). Citric acid and sodium citrate effects on reducing pink color defect of cooked intact turkey breasts and ground turkey rolls. Journal of Food Science, 68, 874-878. (Pubitemid 36453487)
    • (2003) Journal of Food Science , vol.68 , Issue.3 , pp. 874-878
    • Sammel, L.M.1    Claus, J.R.2
  • 22
    • 33744473116 scopus 로고    scopus 로고
    • Redox instability induced by 4-hydroxy-2-nonenal in porcine and bovine myoglobins at pH 5.6 and 4°C
    • DOI 10.1021/jf052811y
    • Suman, S. P., Faustman, C., Stamer, S. L., & Liebler, D. C. (2006). 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, 3402-3408. (Pubitemid 43798212)
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , Issue.9 , pp. 3402-3408
    • Suman, S.P.1    Faustman, C.2    Stamer, S.L.3    Liebler, D.C.4
  • 23
    • 33847627524 scopus 로고    scopus 로고
    • Proteomics of lipid oxidation-induced oxidation of porcine and bovine oxymyoglobins
    • DOI 10.1002/pmic.200600313
    • Suman, S. P., Faustman, C., Stamer, S. L., & Liebler, D. C. (2007). Proteomics of lipid oxidation-induced oxidation in porcine and bovine oxymyoglobins. Proteomics, 7, 628-640. (Pubitemid 46362626)
    • (2007) Proteomics , vol.7 , Issue.4 , pp. 628-640
    • Suman, S.P.1    Faustman, C.2    Stamer, S.L.3    Liebler, D.C.4
  • 25
    • 79958150387 scopus 로고    scopus 로고
    • Amino acid sequence of myoglobin from emu (Dromaius novaehollandiae) skeletal muscle
    • Suman, S. P., Joseph, P., Li, S., Beach, C. M., Steinke, L., & Fontaine, M. (2010). Amino acid sequence of myoglobin from emu (Dromaius novaehollandiae) skeletal muscle. Meat Science, 86, 23-628.
    • (2010) Meat Science , vol.86 , pp. 23-628
    • Suman, S.P.1    Joseph, P.2    Li, S.3    Beach, C.M.4    Steinke, L.5    Fontaine, M.6
  • 26
    • 84866998901 scopus 로고
    • Variation in myoglobin denaturation and color of cooked beef, pork, and turkey meat as influenced by pH, sodium chloride, sodium tripolyphosphate, and cooking temperature
    • Trout, G. R. (1989). 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, 536-544.
    • (1989) Journal of Food Science , vol.54 , pp. 536-544
    • Trout, G.R.1
  • 27
    • 7544236251 scopus 로고    scopus 로고
    • Primary structure and thermostability of bigeye tuna myoglobin in relation to those of other scombridae fish
    • DOI 10.1111/j.1444-2906.2004.00882.x
    • Ueki, N., & Ochiai, Y. (2004). Primary structure and thermostability of bigeye tuna myoglobin in relation to those from other scombridae fish. Fisheries Science, 70, 875-884. (Pubitemid 39448058)
    • (2004) Fisheries Science , vol.70 , Issue.5 , pp. 875-884
    • Ueki, N.1    Ochiai, Y.2
  • 28
    • 21644436544 scopus 로고    scopus 로고
    • Characterization of bullet tuna myoglobin with reference to the thermostability-structure relationship
    • DOI 10.1021/jf050261y
    • Ueki, N., Chow, C. J., & Ochiai, Y. (2005). Characterization of bullet tuna myoglobin with reference to thermostability-structure relationship. Journal of Agricultural and Food Chemistry, 53, 4968-4975. (Pubitemid 40937623)
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.12 , pp. 4968-4975
    • Ueki, N.1    Chow, C.-J.2    Ochiai, Y.3
  • 30
    • 33747844624 scopus 로고    scopus 로고
    • BLAST: Improvements for better sequence analysis
    • DOI 10.1093/nar/gkl164
    • Ye, J., McGinnis, S., & Madden, T. L. (2006). BLAST: Improvements for better sequence analysis. Nucleic Acids Research, 34, W6-W9. (Pubitemid 44529725)
    • (2006) Nucleic Acids Research , vol.34 , Issue.WEB. SERV. ISS
    • Ye, J.1    McGinnis, S.2    Madden, T.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.