메뉴 건너뛰기




Volumn 90, Issue 1, 2012, Pages 77-80

Heat-induced gelation of myosin in a low ionic strength solution containing L-histidine

Author keywords

Binding properties; Heat induced gelation; L histidine; Myosin

Indexed keywords

BINDING PROPERTIES; HIGH IONIC STRENGTH; L-HISTIDINE; LOW IONIC STRENGTH; MEAT PRODUCTS; MYOSIN; OPAQUE GELS; RHEOLOGICAL PROPERTY; STRUCTURAL CHANGE; TRANSPARENT GELS;

EID: 80053187716     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2011.06.002     Document Type: Article
Times cited : (77)

References (15)
  • 1
    • 84981853970 scopus 로고
    • Effect of some proteins on the binding quality of an experimental sausage
    • Fukazawa T., Hashimoto Y., Yasui T. Effect of some proteins on the binding quality of an experimental sausage. Journal of Food Science 1961, 26:541-549.
    • (1961) Journal of Food Science , vol.26 , pp. 541-549
    • Fukazawa, T.1    Hashimoto, Y.2    Yasui, T.3
  • 2
    • 62349085423 scopus 로고    scopus 로고
    • Myosin is solubilized in a neutral and low ionic strength solution containing L-histidine
    • Hayakawa T., Ito T., Wakamatsu J., Nishimura T., Hattori A. Myosin is solubilized in a neutral and low ionic strength solution containing L-histidine. Meat Science 2009, 82:151-154.
    • (2009) Meat Science , vol.82 , pp. 151-154
    • Hayakawa, T.1    Ito, T.2    Wakamatsu, J.3    Nishimura, T.4    Hattori, A.5
  • 3
    • 76449108928 scopus 로고    scopus 로고
    • Myosin filament depolymerizes in a low ionic strength solution containing L-histidine
    • Hayakawa T., Ito T., Wakamatsu J., Nishimura T., Hattori A. Myosin filament depolymerizes in a low ionic strength solution containing L-histidine. Meat Science 2010, 84:742-746.
    • (2010) Meat Science , vol.84 , pp. 742-746
    • Hayakawa, T.1    Ito, T.2    Wakamatsu, J.3    Nishimura, T.4    Hattori, A.5
  • 4
    • 84985262237 scopus 로고
    • Heat-induced gelation of myosin: Factors of pH and Salt concentrations
    • Ishioroshi M., Samejima K., Yasui T. Heat-induced gelation of myosin: Factors of pH and Salt concentrations. Journal of Food Science 1979, 44:1280-1284.
    • (1979) Journal of Food Science , vol.44 , pp. 1280-1284
    • Ishioroshi, M.1    Samejima, K.2    Yasui, T.3
  • 5
    • 84985225735 scopus 로고
    • Further studies on the roles of the head and tail regions of the myosin molecule in heat-induced gelation
    • Ishioroshi M., Samejima K., Yasui T. Further studies on the roles of the head and tail regions of the myosin molecule in heat-induced gelation. Journal of Food Science 1981, 47:114-120.
    • (1981) Journal of Food Science , vol.47 , pp. 114-120
    • Ishioroshi, M.1    Samejima, K.2    Yasui, T.3
  • 6
    • 0242657344 scopus 로고    scopus 로고
    • The solubilization of myofibrillar proteins of vertebrate skeletal muscle in water
    • Ito Y., Tatsumi R., Wakamatsu J., Nishimura T., Hattori A. The solubilization of myofibrillar proteins of vertebrate skeletal muscle in water. Animal Science Journal 2003, 74:417-425.
    • (2003) Animal Science Journal , vol.74 , pp. 417-425
    • Ito, Y.1    Tatsumi, R.2    Wakamatsu, J.3    Nishimura, T.4    Hattori, A.5
  • 7
    • 50249126674 scopus 로고    scopus 로고
    • Role of secondary structures in the gelation of porcine myosin at different pH values
    • Liu R., Zhao S., Xiong S., Xie B., Qin L. Role of secondary structures in the gelation of porcine myosin at different pH values. Meat Science 2008, 80:632-639.
    • (2008) Meat Science , vol.80 , pp. 632-639
    • Liu, R.1    Zhao, S.2    Xiong, S.3    Xie, B.4    Qin, L.5
  • 8
    • 77956984659 scopus 로고
    • Myosin adenosinetriphosphatase
    • Perry S.V. Myosin adenosinetriphosphatase. Methods in Enzymology 1955, 2:582-588.
    • (1955) Methods in Enzymology , vol.2 , pp. 582-588
    • Perry, S.V.1
  • 9
    • 77954383543 scopus 로고    scopus 로고
    • Theoretical aspects of water-holding in meat
    • Puolanne E., Halonen M. Theoretical aspects of water-holding in meat. Meat Science 2010, 86:151-165.
    • (2010) Meat Science , vol.86 , pp. 151-165
    • Puolanne, E.1    Halonen, M.2
  • 10
    • 35448952867 scopus 로고    scopus 로고
    • Conformational and rheological changes in catfish myosin during alkali-induced unfolding and refolding
    • Raghavan S., Kristinsson H.K. Conformational and rheological changes in catfish myosin during alkali-induced unfolding and refolding. Food Chemistry 2008, 107:385-398.
    • (2008) Food Chemistry , vol.107 , pp. 385-398
    • Raghavan, S.1    Kristinsson, H.K.2
  • 11
    • 39149097500 scopus 로고    scopus 로고
    • Comparative study on acid-induced gelation of myosin from Atlantic cod (Gardus morhua) and burbot (Lota lota)
    • Riebroy S., Benjakul S., Visessanguan W., Erikson U., Rustad T. Comparative study on acid-induced gelation of myosin from Atlantic cod (Gardus morhua) and burbot (Lota lota). Food Chemistry 2008, 109:42-53.
    • (2008) Food Chemistry , vol.109 , pp. 42-53
    • Riebroy, S.1    Benjakul, S.2    Visessanguan, W.3    Erikson, U.4    Rustad, T.5
  • 12
    • 84989992648 scopus 로고
    • Heat gelling properties of myosin, actin, actomyosin and myosin-subunits in saline model system
    • Samejima K., Hashimoto Y., Yasui T., Fukazawa T. Heat gelling properties of myosin, actin, actomyosin and myosin-subunits in saline model system. Journal of Food Science 1969, 34:242-245.
    • (1969) Journal of Food Science , vol.34 , pp. 242-245
    • Samejima, K.1    Hashimoto, Y.2    Yasui, T.3    Fukazawa, T.4
  • 13
    • 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. Journal of Food Science 1981, 46:1412-1418.
    • (1981) Journal of Food Science , vol.46 , pp. 1412-1418
    • Samejima, K.1    Ishioroshi, M.2    Yasui, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.