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Volumn 63, Issue 2, 1997, Pages 237-241

The subfragment responsible for the polymerization of myosin heavy chain through SS bonding during the heating of carp myosin

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EID: 21744458890     PISSN: 00215392     EISSN: None     Source Type: Journal    
DOI: 10.2331/suisan.63.237     Document Type: Article
Times cited : (7)

References (16)
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  • 3
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    • The sulfhydryl groups involved in the active site of myosin B adenosine triphosphatase
    • T. Yamashita, M. Kobayashi, and T. Horigome: The sulfhydryl groups involved in the active site of myosin B adenosine triphosphatase. J. Biochem., 77, 1037-1046 (1975).
    • (1975) J. Biochem. , vol.77 , pp. 1037-1046
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  • 4
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    • Relative roles of the head and tail portions of the molecule in heat-induced gelation of myosin
    • K. Samejima, M. Ishioroshi, and T. Yasui: Relative roles of the head and tail portions of the molecule in heat-induced gelation of myosin. J. Food Sci., 46, 1412-1423 (1981).
    • (1981) J. Food Sci. , vol.46 , pp. 1412-1423
    • Samejima, K.1    Ishioroshi, M.2    Yasui, T.3
  • 5
    • 0001048082 scopus 로고    scopus 로고
    • a in the polymerization of myosin heavy chain during ice storage of carp actomyosin
    • a in the polymerization of myosin heavy chain during ice storage of carp actomyosin. Fisheries Sci., 62, 110-113 (1996).
    • (1996) Fisheries Sci. , vol.62 , pp. 110-113
    • Sompongse, W.1    Itoh, Y.2    Obatake, A.3
  • 6
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    • Responsibility of myosin rod for the dimer formation of myosin heavy chain through SS bonding during ice storage of carp actomyosin
    • W. Sompongse, Y. Itoh, and A. Obatake: Responsibility of myosin rod for the dimer formation of myosin heavy chain through SS bonding during ice storage of carp actomyosin. Fisheries Sci., 62, 473-477 (1996).
    • (1996) Fisheries Sci. , vol.62 , pp. 473-477
    • Sompongse, W.1    Itoh, Y.2    Obatake, A.3
  • 7
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    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • K. Weber and M. Osborn: The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem., 224, 4406-4412.
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  • 13
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    • Tissue sulfhydryl groups
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  • 15
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    • Hydrostatic pressure-induced aggregation of myosin molecules in 0.5 M KCl at pH 6.0
    • K. Yamamoto, S. Hayashi, and T. Yasui: Hydrostatic pressure-induced aggregation of myosin molecules in 0.5 M KCl at pH 6.0. Biosci. Biotech. Biochem., 57, 383-389 (1993).
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 383-389
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  • 16
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    • Structural changes of carp myosin during heating
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.