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Volumn 44, Issue 10, 1996, Pages 2944-2945

α-Helical Structure of Fish Actomyosin Changes during Storage

Author keywords

Actomyosin; Circular dichroism; Fish; Myosin; Preparation; helix

Indexed keywords


EID: 0000388799     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf960229r     Document Type: Article
Times cited : (11)

References (22)
  • 2
    • 38249015395 scopus 로고
    • Thermal denaturation of turkey breast myosin under different conditions: Effect of temperature and pH, and reversibility of the denaturation
    • Arteaga, G. E.; Nakai, S. Thermal denaturation of turkey breast myosin under different conditions: effect of temperature and pH, and reversibility of the denaturation. Meat Sci. 1992, 31, 191-200.
    • (1992) Meat Sci. , vol.31 , pp. 191-200
    • Arteaga, G.E.1    Nakai, S.2
  • 3
    • 0024786754 scopus 로고
    • Thermal aggregation of cod (Gadus morhua) muscle proteins using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a zero length cross-linker
    • Gill, T. A.; Conway, J. T. Thermal aggregation of cod (Gadus morhua) muscle proteins using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a zero length cross-linker. Agric. biol. Chem. 1989, 53, 2553-2562.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 2553-2562
    • Gill, T.A.1    Conway, J.T.2
  • 4
    • 0016713965 scopus 로고
    • Thermodynamic activation parameters of fish myofibrillar ATPase enzyme and evolutionary adaptations to temperature
    • Johnston, I. A.; Goldspink, G. Thermodynamic activation parameters of fish myofibrillar ATPase enzyme and evolutionary adaptations to temperature. Nature 1975, 257, 620-622.
    • (1975) Nature , vol.257 , pp. 620-622
    • Johnston, I.A.1    Goldspink, G.2
  • 5
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 8
    • 85032068662 scopus 로고
    • Structural changes of carp myosin during heating
    • Ogawa, M.; Tamiya, T.; Tsuchiya, T. Structural changes of carp myosin during heating. Fish. Sci. 1994, 60, 723-727.
    • (1994) Fish. Sci. , vol.60 , pp. 723-727
    • Ogawa, M.1    Tamiya, T.2    Tsuchiya, T.3
  • 9
    • 84986436002 scopus 로고
    • Alpha-helical structure of fish actomyosin: Changes during setting
    • Ogawa, M.; Kanamaru, J.; Miyashita, H.; Tamiya, T.; Tsuchiya, T. Alpha-helical structure of fish actomyosin: changes during setting. J. Food Sci. 1995, 60, 297-299.
    • (1995) J. Food Sci. , vol.60 , pp. 297-299
    • Ogawa, M.1    Kanamaru, J.2    Miyashita, H.3    Tamiya, T.4    Tsuchiya, T.5
  • 10
    • 84989992648 scopus 로고
    • Heating gelling properties of myosin, actin, actomyosin and myosin-subunits in a saline model system
    • Samejimna, K.; Hashimoto, Y.; Yasui, T.; Fukuzawa, T. Heating gelling properties of myosin, actin, actomyosin and myosin-subunits in a saline model system. J. Food Sci. 1969, 34, 242-245.
    • (1969) J. Food Sci. , vol.34 , pp. 242-245
    • Samejimna, K.1    Hashimoto, Y.2    Yasui, T.3    Fukuzawa, T.4
  • 11
    • 84952398782 scopus 로고
    • Relative roles of the head and tail portions of the molecule in heat-induced gelation of myosin
    • Samejima, K.; Ishioroshi, M.; Yasui, T. Relative roles of the head and tail portions of the molecule in heat-induced gelation of myosin. J. Food Sci. 1981, 46, 1412-1418.
    • (1981) J. Food Sci. , vol.46 , pp. 1412-1418
    • Samejima, K.1    Ishioroshi, M.2    Yasui, T.3
  • 12
    • 84861673615 scopus 로고
    • Contribution of paramyosin to marine meat gel characteristics
    • Sano, T.; Noguchi, S. F.; Tsuchiya, T.; Matsumoto, J. J. Contribution of paramyosin to marine meat gel characteristics. J. Food Sci. 1986, 51, 946-950.
    • (1986) J. Food Sci. , vol.51 , pp. 946-950
    • Sano, T.1    Noguchi, S.F.2    Tsuchiya, T.3    Matsumoto, J.J.4
  • 13
    • 84971620957 scopus 로고
    • Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation
    • Sano, T.; Noguchi, S. F.; Tsuchiya, T.; Matsumoto, J. J. Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation. J. Food Sci. 1988, 53, 924-928.
    • (1988) J. Food Sci. , vol.53 , pp. 924-928
    • Sano, T.1    Noguchi, S.F.2    Tsuchiya, T.3    Matsumoto, J.J.4
  • 14
    • 84987368757 scopus 로고
    • Effect of ionic strength on dynamic viscoelastic behavior of myosin during thermal gelation
    • Sano, T.; Noguchi, S. F.; Matsumoto, J. J.; Tsuchiya, T. Effect of ionic strength on dynamic viscoelastic behavior of myosin during thermal gelation. J. Food Sci. 1990, 55, 51-54.
    • (1990) J. Food Sci. , vol.55 , pp. 51-54
    • Sano, T.1    Noguchi, S.F.2    Matsumoto, J.J.3    Tsuchiya, T.4
  • 15
    • 0002125934 scopus 로고
    • The mechanism of formation of gels from myosin molecules
    • Sharp, A.; Offer, G. The mechanism of formation of gels from myosin molecules. J. Sci. Food Agric. 1992, 58, 63-73.
    • (1992) J. Sci. Food Agric. , vol.58 , pp. 63-73
    • Sharp, A.1    Offer, G.2
  • 16
  • 18
    • 0000741849 scopus 로고
    • Dynamic rheological properties and secondary structure of chicken breast myosin as influenced by isothermal heating
    • Wang, S. F.; Smith, D. M. Dynamic rheological properties and secondary structure of chicken breast myosin as influenced by isothermal heating. J. Agric. Food Chem. 1994, 42, 1434-1439.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1434-1439
    • Wang, S.F.1    Smith, D.M.2
  • 19
    • 0024109903 scopus 로고
    • The binding of 8-anilino-1-naphthalene sulfonate (ANS) to fish myosin and the effect of salts on the thermal transitions of fish myosin-ANS complex
    • Wicker, L.; Knopp, J. A. The binding of 8-anilino-1-naphthalene sulfonate (ANS) to fish myosin and the effect of salts on the thermal transitions of fish myosin-ANS complex. Arch. Biochem. Biophys. 1988, 266, 452-461.
    • (1988) Arch. Biochem. Biophys. , vol.266 , pp. 452-461
    • Wicker, L.1    Knopp, J.A.2
  • 20
    • 0021396951 scopus 로고
    • Differential scanning calorimetric study of muscle and its proteins: Myosin and its subfragments
    • Wright, D. J.; Wilding, P. Differential scanning calorimetric study of muscle and its proteins: myosin and its subfragments. J. Sci. Food Agric. 1984, 35, 357-372.
    • (1984) J. Sci. Food Agric. , vol.35 , pp. 357-372
    • Wright, D.J.1    Wilding, P.2
  • 21
    • 0003200724 scopus 로고
    • Myosin gelation kinetics study based on rheological measurements
    • Wu, J. Q.; Hamann, D. D.; Foegeding, E. A. Myosin gelation kinetics study based on rheological measurements. J. Agric. Food Chem. 1991, 39, 229-236.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 229-236
    • Wu, J.Q.1    Hamann, D.D.2    Foegeding, E.A.3
  • 22
    • 0019971078 scopus 로고
    • Effect of actomyosin on heat-induced gelation of myosin
    • Yasui, T.; Ishioroshi, M.; Samajima, K. Effect of actomyosin on heat-induced gelation of myosin. Agric. Biol. Chem. 1982, 46, 1049-1059.
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 1049-1059
    • Yasui, T.1    Ishioroshi, M.2    Samajima, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.