메뉴 건너뛰기




Volumn 71, Issue 3, 2006, Pages

Identification of cross-linking site(s) of myosin heavy chains in oxidatively stressed chicken myofibrils

Author keywords

Chymotryptic digestion; Cross linking; Disulfide bond; Myosin; Oxidation

Indexed keywords


EID: 33646381930     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2006.tb15617.x     Document Type: Article
Times cited : (54)

References (17)
  • 1
    • 84985262237 scopus 로고
    • Teat-induced gelation of myosin. Factors of pH and salt concentrations
    • Ishioroshi M, Samejima K, Yasui. 1979. Teat-induced gelation of myosin. Factors of pH and salt concentrations. J Food Sci 44:1280-4.
    • (1979) J Food Sci , vol.44 , pp. 1280-1284
    • Ishioroshi, M.1    Samejima, K.2    Yasui3
  • 2
    • 0001460366 scopus 로고    scopus 로고
    • Oligomerization of carp myosin which retains its ATPase activity
    • Kato S, Koseki H, Konno K. 1996. Oligomerization of carp myosin which retains its ATPase activity. Fish Sci 62:985-9.
    • (1996) Fish Sci , vol.62 , pp. 985-989
    • Kato, S.1    Koseki, H.2    Konno, K.3
  • 4
    • 0033789561 scopus 로고    scopus 로고
    • Early structural changes myosin rod upon heating of carp myofibrils
    • Konno K, Yamamoto T, Takahashi M, Kato S. 2000. Early structural changes myosin rod upon heating of carp myofibrils. J Agric Food Chem 48:4905-9.
    • (2000) J Agric Food Chem , vol.48 , pp. 4905-4909
    • Konno, K.1    Yamamoto, T.2    Takahashi, M.3    Kato, S.4
  • 5
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, K.1
  • 6
    • 0034127455 scopus 로고    scopus 로고
    • Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin
    • Liu G, Xiong YL. 2000a. Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin. J Agric Food Chem 48:624-30.
    • (2000) J Agric Food Chem , vol.48 , pp. 624-630
    • Liu, G.1    Xiong, Y.L.2
  • 7
    • 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, Xiong YL. 2000b. Thermal transitions and dynamic gelling properties of oxidatively modified myosin, β-lactoglobulin, soy 7S globulin and their mixtures. J Sci Food Agric 80:1728-34.
    • (2000) J Sci Food Agric , vol.80 , pp. 1728-1734
    • Liu, G.1    Xiong, Y.L.2
  • 8
    • 0033827809 scopus 로고    scopus 로고
    • Chemical, physical, and gel-forming properties of oxidized myofibrils and whey- and soy-protein isolate
    • Liu G, Xiong YL, Butterfield DA. 2000. Chemical, physical, and gel-forming properties of oxidized myofibrils and whey- and soy-protein isolate. J Food Sci 65:811-7.
    • (2000) J Food Sci , vol.65 , pp. 811-817
    • Liu, G.1    Xiong, Y.L.2    Butterfield, D.A.3
  • 9
    • 0025826377 scopus 로고
    • The primary structure of skeletal muscle myosin heavy chain: IV. Sequence of rod, and the complete 1,938-residue sequence of the heavy chain
    • Maita T, Yajima T, Nagata S, Miyanishi T, Nakayama S, Matsuda G. 1991. The primary structure of skeletal muscle myosin heavy chain: IV. Sequence of rod, and the complete 1,938-residue sequence of the heavy chain. J Biochem 110:75-87.
    • (1991) J Biochem , vol.110 , pp. 75-87
    • Maita, T.1    Yajima, T.2    Nagata, S.3    Miyanishi, T.4    Nakayama, S.5    Matsuda, G.6
  • 10
    • 3042518998 scopus 로고    scopus 로고
    • Biochemical susceptibility of myosin in chicken myofibrils subjected to hydroxyl radical oxidizing systems
    • Ooizumi T, Xiong YL. 2004. Biochemical susceptibility of myosin in chicken myofibrils subjected to hydroxyl radical oxidizing systems. J Agric Food Chem 52:4303-7.
    • (2004) J Agric Food Chem , vol.52 , pp. 4303-4307
    • Ooizumi, T.1    Xiong, Y.L.2
  • 12
    • 0002125934 scopus 로고
    • The mechanism of formation of gels from myosin molecules
    • Sharp A, Offer G. 1992 The mechanism of formation of gels from myosin molecules. J Sci Food Agric 58:68-73.
    • (1992) J Sci Food Agric , vol.58 , pp. 68-73
    • Sharp, A.1    Offer, G.2
  • 13
    • 0009783999 scopus 로고    scopus 로고
    • Responsibility of myosin rod for the dimer formation of myosin heavy chain through SS bonding during ice storage of carp actomyosin
    • Sompongse W, Itoh Y, Obatake A. 1996. Responsibility of myosin rod for the dimer formation of myosin heavy chain through SS bonding during ice storage of carp actomyosin. Fish Sci 62:473-7.
    • (1996) Fish Sci , vol.62 , pp. 473-477
    • Sompongse, W.1    Itoh, Y.2    Obatake, A.3
  • 14
    • 0000933366 scopus 로고    scopus 로고
    • Chemical, physical, and functional properties of cod proteins modified by a nonenzymic free-radical-generating system
    • Srinivasan S, Hultin HO. 1997. Chemical, physical, and functional properties of cod proteins modified by a nonenzymic free-radical-generating system. J Agric Food Chem 45:310-20.
    • (1997) J Agric Food Chem , vol.45 , pp. 310-320
    • Srinivasan, S.1    Hultin, H.O.2
  • 15
    • 0036006643 scopus 로고    scopus 로고
    • Role of neck region in the fermai aggregation of myosin
    • Tazawa T, Kato S, Katoh T, Konno K. 2002. Role of neck region in the fermai aggregation of myosin. J Agric Food Chem 50:196-202.
    • (2002) J Agric Food Chem , vol.50 , pp. 196-202
    • Tazawa, T.1    Kato, S.2    Katoh, T.3    Konno, K.4
  • 16
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin. Effect of divalent cations on proteolytic susceptibility
    • Weeds A, Pope B. 1977. Studies on the chymotryptic digestion of myosin. Effect of divalent cations on proteolytic susceptibility. J Mol Biol 111:129-57.
    • (1977) J Mol Biol , vol.111 , pp. 129-157
    • Weeds, A.1    Pope, B.2
  • 17
    • 0025607119 scopus 로고
    • Electron microscopy of thermal aggregation of myosin
    • Yamamoto K. 1990. Electron microscopy of thermal aggregation of myosin. J Biochem 108:896-8.
    • (1990) J Biochem , vol.108 , pp. 896-898
    • Yamamoto, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.