메뉴 건너뛰기




Volumn 106, Issue 2, 2008, Pages 661-668

Hydroxyl radical oxidation destabilizes subfragment-1 but not the rod of myosin in chicken myofibrils

Author keywords

Ca ATPase; Chymotryptic digestibility; Denaturation; Myofibrils; Myosin; Oxidation; Salt solubility

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); HYDROXYL RADICAL; MYOSIN;

EID: 34548226860     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2007.06.029     Document Type: Article
Times cited : (9)

References (28)
  • 3
    • 0001460366 scopus 로고    scopus 로고
    • Oligomerization of carp myosin which retains its ATPase activity
    • Kato S., Koseki H., and Konno K. Oligomerization of carp myosin which retains its ATPase activity. Fisheries Science 62 (1996) 985-989
    • (1996) Fisheries Science , vol.62 , pp. 985-989
    • Kato, S.1    Koseki, H.2    Konno, K.3
  • 5
    • 85009578852 scopus 로고
    • Mg-ATPase enhancement of carp myofibrils upon thermal treatment
    • Konno K., and Ueda Y. Mg-ATPase enhancement of carp myofibrils upon thermal treatment. Nippon Suisan Gakkaishi 55 (1989) 1457-1462
    • (1989) Nippon Suisan Gakkaishi , vol.55 , pp. 1457-1462
    • Konno, K.1    Ueda, Y.2
  • 7
    • 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 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 8
    • 13044311380 scopus 로고    scopus 로고
    • Structural changes of rabbit myosin subfragement 1 altered by malonaldehyde, a byproduct of lipid oxidation
    • Li S.J., and King A.J. Structural changes of rabbit myosin subfragement 1 altered by malonaldehyde, a byproduct of lipid oxidation. Journal of Agricultural and Food Chemistry 47 (1999) 3124-3129
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , pp. 3124-3129
    • Li, S.J.1    King, A.J.2
  • 9
    • 0034127455 scopus 로고    scopus 로고
    • Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin
    • Liu G., and Xiong Y.L. Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin. Journal of Agricultural and Food Chemistry 48 (2000) 624-630
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 624-630
    • Liu, G.1    Xiong, Y.L.2
  • 10
    • 0034666486 scopus 로고    scopus 로고
    • Thermal transitions and dynamic gelling properties of oxidatively modified myosin, β-lactoglobulin, soy 7S globulin and their mixtures
    • Liu G., and Xiong Y.L. Thermal transitions and dynamic gelling properties of oxidatively modified myosin, β-lactoglobulin, soy 7S globulin and their mixtures. Journal of the Science of Food and Agriculture 80 (2000) 1728-1734
    • (2000) Journal of the Science of Food and Agriculture , vol.80 , pp. 1728-1734
    • Liu, G.1    Xiong, Y.L.2
  • 11
  • 12
    • 84998226449 scopus 로고
    • Comparative study on the enzymatic properties and thermal stabilities of N-ethylmaleimide modified myosins from fish dorsal and rabbit skeletal muscles
    • Murozuka T. Comparative study on the enzymatic properties and thermal stabilities of N-ethylmaleimide modified myosins from fish dorsal and rabbit skeletal muscles. Nippon Suisan Gakkaishi 45 (1979) 1503-1512
    • (1979) Nippon Suisan Gakkaishi , vol.45 , pp. 1503-1512
    • Murozuka, T.1
  • 13
    • 3042518998 scopus 로고    scopus 로고
    • Biochemical susceptibility of myosin in chicken myofibrils subjected to hydroxyl radical oxidizing systems
    • Ooizumi T., and Xiong Y.L. Biochemical susceptibility of myosin in chicken myofibrils subjected to hydroxyl radical oxidizing systems. Journal of Agricultural and Food Chemistry 52 (2004) 4303-4307
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 4303-4307
    • Ooizumi, T.1    Xiong, Y.L.2
  • 14
    • 33646381930 scopus 로고    scopus 로고
    • Identification of cross-linking site(s) of myosin heavy chains in oxidatively stressed chicken myofibrils
    • Ooizumi T., and Xiong Y.L. Identification of cross-linking site(s) of myosin heavy chains in oxidatively stressed chicken myofibrils. Journal of Food Science 71 (2006) C196-C199
    • (2006) Journal of Food Science , vol.71
    • Ooizumi, T.1    Xiong, Y.L.2
  • 15
    • 3042529321 scopus 로고
    • Effect of ATP on the binding of N-ethylmaleimide to SH groups in the active site of myosin ATPase
    • Sekine T., and Yamaguchi M. Effect of ATP on the binding of N-ethylmaleimide to SH groups in the active site of myosin ATPase. Journal of Biochemistry 54 (1963) 196-198
    • (1963) Journal of Biochemistry , vol.54 , pp. 196-198
    • Sekine, T.1    Yamaguchi, M.2
  • 17
    • 84985275078 scopus 로고
    • Functional and biochemical changes in deboned turkey due to frozen storage and lipid oxidation
    • Smith D.M. Functional and biochemical changes in deboned turkey due to frozen storage and lipid oxidation. Journal of Food Science 52 (1987) 22-27
    • (1987) Journal of Food Science , vol.52 , pp. 22-27
    • Smith, D.M.1
  • 18
    • 0000933366 scopus 로고    scopus 로고
    • Chemical, physical, and functional properties of cod proteins modified by a nonenzymic free-radical-generating system
    • Srinivasan S., and Hultin H.O. Chemical, physical, and functional properties of cod proteins modified by a nonenzymic free-radical-generating system. Journal of Agricultural and Food Chemistry 45 (1997) 310-320
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 310-320
    • Srinivasan, S.1    Hultin, H.O.2
  • 19
    • 18844431101 scopus 로고    scopus 로고
    • Species-specific thermal denaturation pattern of fish myosin when heated as myofibrils as studied by myosin subfragment-1 and rod denaturation rates
    • Takahashi M., Yamamoto T., Kato S., and Konno K. Species-specific thermal denaturation pattern of fish myosin when heated as myofibrils as studied by myosin subfragment-1 and rod denaturation rates. Fisheries Science 71 (2005) 405-413
    • (2005) Fisheries Science , vol.71 , pp. 405-413
    • Takahashi, M.1    Yamamoto, T.2    Kato, S.3    Konno, K.4
  • 21
    • 85008121459 scopus 로고
    • Effect of neutral salts on thermal denaturation of myofibrillar Ca-ATPase of Fish
    • Wakameda A., Nozawa S., and Arai K. Effect of neutral salts on thermal denaturation of myofibrillar Ca-ATPase of Fish. Nippon Suisan Gakkaishi 49 (1983) 237-243
    • (1983) Nippon Suisan Gakkaishi , vol.49 , pp. 237-243
    • Wakameda, A.1    Nozawa, S.2    Arai, K.3
  • 22
    • 0000989650 scopus 로고
    • Inhibition of oxidation during washing improves the functionality of bovine cardiac myofibrillar protein
    • Wan L., Xiong Y.L., and Decker E.A. Inhibition of oxidation during washing improves the functionality of bovine cardiac myofibrillar protein. Journal of Agricultural and Food Chemistry 41 (1993) 2267-2271
    • (1993) Journal of Agricultural and Food Chemistry , vol.41 , pp. 2267-2271
    • Wan, L.1    Xiong, Y.L.2    Decker, E.A.3
  • 23
    • 0031925483 scopus 로고    scopus 로고
    • Functional stability of antioxidant-washed, cryoprotectant - treated beef heart surimi during frozen storage
    • Wang B., and Xiong Y.L. Functional stability of antioxidant-washed, cryoprotectant - treated beef heart surimi during frozen storage. Journal of Food Science 63 (1998) 293-298
    • (1998) Journal of Food Science , vol.63 , pp. 293-298
    • Wang, B.1    Xiong, Y.L.2
  • 24
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin. Effect of divalent cations on proteolytic susceptibility
    • Weeds A., and Pope B. Studies on the chymotryptic digestion of myosin. Effect of divalent cations on proteolytic susceptibility. Journal of Molecular Biology 111 (1977) 129-157
    • (1977) Journal of Molecular Biology , vol.111 , pp. 129-157
    • Weeds, A.1    Pope, B.2
  • 25
    • 0000417085 scopus 로고
    • Gelation of crude myofibrillar protein isolated from beef heart under antioxidative conditions
    • Xiong Y.L., Decker E.A., Robe G.H., and Moody W.G. Gelation of crude myofibrillar protein isolated from beef heart under antioxidative conditions. Journal of Food Science 58 (1993) 1241-1244
    • (1993) Journal of Food Science , vol.58 , pp. 1241-1244
    • Xiong, Y.L.1    Decker, E.A.2    Robe, G.H.3    Moody, W.G.4
  • 26
    • 0025607119 scopus 로고
    • Electron microscopy of thermal aggregation of myosin
    • Yamamoto K. Electron microscopy of thermal aggregation of myosin. Journal of Biochemistry 108 (1990) 896-898
    • (1990) Journal of Biochemistry , vol.108 , pp. 896-898
    • Yamamoto, K.1
  • 27
    • 0036311046 scopus 로고    scopus 로고
    • Denaturation mode of carp myofibrils when affected by temperature and salt concentration
    • Yamamoto Y., Takahashi M., Kato S., and Konno K. Denaturation mode of carp myofibrils when affected by temperature and salt concentration. Fisheries Science 68 (2002) 627-633
    • (2002) Fisheries Science , vol.68 , pp. 627-633
    • Yamamoto, Y.1    Takahashi, M.2    Kato, S.3    Konno, K.4
  • 28
    • 10544226427 scopus 로고
    • Thermal inactivation of myosin A adenosine triphosphatase in the presence of F-actin
    • Yasui T., Kawakami H., and Morita F. Thermal inactivation of myosin A adenosine triphosphatase in the presence of F-actin. Agricultural Biological Chemistry 32 (1968) 225-233
    • (1968) Agricultural Biological Chemistry , vol.32 , pp. 225-233
    • Yasui, T.1    Kawakami, H.2    Morita, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.