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Volumn 68, Issue , 2002, Pages 1545-1548

Comparison in thermodynamic and viscoelastic properties of fast skeletal myosin between walleye pollack and white croaker

Author keywords

DSC; loss modulus; myosin; storage modulus; tan ; thermal gel; unfolding

Indexed keywords


EID: 0038293839     PISSN: 09199268     EISSN: 14442906     Source Type: Journal    
DOI: 10.2331/fishsci.68.sup2_1545     Document Type: Article
Times cited : (1)

References (27)
  • 1
    • 0005184257 scopus 로고
    • Kamaboko formation of mackerel and red sea bream myosins
    • Iwata K., Kanna K., Okada M. Kamaboko formation of mackerel and red sea bream myosins. Nippon Suisan Gakkaishi 1977; 43: 237.
    • (1977) Nippon Suisan Gakkaishi , vol.43 , pp. 237
    • Iwata, K.1    Kanna, K.2    Okada, M.3
  • 5
    • 84987301296 scopus 로고
    • Action of crude papain on actin and myosin heavy chains isolated from chicken breast muscle.
    • Rattrie N. W., Regenstein J. M. Action of crude papain on actin and myosin heavy chains isolated from chicken breast muscle. J. FoodSci. 1977; 42: 1159–1163.
    • (1977) J. FoodSci. , vol.42 , pp. 1159-1163
    • Rattrie, N.W.1    Regenstein, J.M.2
  • 6
    • 85008140040 scopus 로고
    • Electron microscopic study of fine structure of kamaboko fish jellies
    • Satoh S., Tsuchiya T., Matsumoto J. J. Electron microscopic study of fine structure of kamaboko fish jellies. Nippon Suisan Gakkaishi 1984; 50: 1976–1986.
    • (1984) Nippon Suisan Gakkaishi , vol.50 , pp. 1976-1986
    • Satoh, S.1    Tsuchiya, T.2    Matsumoto, J.J.3
  • 7
    • 85008538342 scopus 로고
    • Electron microscopic study of dispersion profiles of proteins in frozen surimi
    • Satoh S., Tsuchiya T., Matsumoto J. J. Electron microscopic study of dispersion profiles of proteins in frozen surimi. Nippon Suisan Gakkaishi 1984; 50: 2117–5126.
    • (1984) Nippon Suisan Gakkaishi , vol.50 , pp. 2117-5126
    • Satoh, S.1    Tsuchiya, T.2    Matsumoto, J.J.3
  • 8
    • 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
  • 9
    • 84971620957 scopus 로고
    • Dynamic viscoelastic behavior of natual actomyosin and myosin during thermal gelation.
    • Sano T., Noguchi S., Tsuchiya T., Matsumoto J. J. Dynamic viscoelastic behavior of natual 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.2    Tsuchiya, T.3    Matsumoto, J.J.4
  • 10
    • 0018609597 scopus 로고
    • Regulatory properties of single-headed fragments of scallop myosin
    • Stafford W. F.III, Szentkiralyi E. M., Szent-Gyorgyi A. G. Regulatory properties of single-headed fragments of scallop myosin. Biochemistry 1979; 18: 5273–5280.
    • (1979) Biochemistry , vol.18 , pp. 5273-5280
    • Stafford, W.F.1    Szentkiralyi, E.M.2    Szent-Gyorgyi, A.G.3
  • 11
    • 0000678368 scopus 로고
    • Changes of carp myosin subfragment-1 induced by temperature acclimation
    • Hwang G. C., Watabe S., Hashimoto K. Changes of carp myosin subfragment-1 induced by temperature acclimation. J. Comp. Physiol. B 1990; 160:141–146.
    • (1990) J. Comp. Physiol. B , vol.160 , pp. 141-146
    • Hwang, G.C.1    Watabe, S.2    Hashimoto, K.3
  • 13
    • 29744466425 scopus 로고
    • Determination of serum proteins by meams of biuret reaction.
    • Gornall A. G., Bardawill C. J., David M. M. Determination of serum proteins by meams of biuret reaction. J. Biol. Chem. 1949; 177: 751–765.
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-765
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 14
    • 0028913571 scopus 로고
    • Differences in the thermal stability of acclimation temperature-associated types of carp myosin and its rod on differential scanning calorimetry
    • Nakaya M., Watabe S., Ooi T. Differences in the thermal stability of acclimation temperature-associated types of carp myosin and its rod on differential scanning calorimetry. Biochemisty 1995; 34: 3114–3120.
    • (1995) Biochemisty , vol.34 , pp. 3114-3120
    • Nakaya, M.1    Watabe, S.2    Ooi, T.3
  • 15
    • 21844508379 scopus 로고
    • Rheological parameters as predictor of protein functionary-A model study using myofibrils of different fiber-type composition.
    • Egelandsdal B., Martinsen B., Autio K. Rheological parameters as predictor of protein functionary-A model study using myofibrils of different fiber-type composition. Meat Sci. 1995;39:97–111.
    • (1995) Meat Sci. , vol.39 , pp. 97-111
    • Egelandsdal, B.1    Martinsen, B.2    Autio, K.3
  • 16
    • 0000358270 scopus 로고
    • Role of the thermal denaturation-aggregation relationship in determining the rheological properties of heat induced networks for ovalbumin and vicilin.
    • Arntfild S. D., Murray E. D., Ismond M. A. H., Bernatsky A. M. Role of the thermal denaturation-aggregation relationship in determining the rheological properties of heat induced networks for ovalbumin and vicilin. J. Food Sci. 1989; 54: 1624–1631.
    • (1989) J. Food Sci. , vol.54 , pp. 1624-1631
    • Arntfild, S.D.1    Murray, E.D.2    Ismond, M.A.H.3    Bernatsky, A.M.4
  • 17
    • 0034055958 scopus 로고    scopus 로고
    • Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin.
    • Visessanguan W., Ogawa M., Nakai S., An H. Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin. J. Agric. Food Chem. 2000; 48: 1016–1023.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 1016-1023
    • Visessanguan, W.1    Ogawa, M.2    Nakai, S.3    An, H.4
  • 19
    • 84986736089 scopus 로고
    • Relationship between functional and physicochemical properties of muscle proteins.
    • Li-Chan E., Nakai S., Wood D. Relationship between functional and physicochemical properties of muscle proteins. J. Food Sci. 1985; 50: 1034–1040.
    • (1985) J. Food Sci. , vol.50 , pp. 1034-1040
    • Li-Chan, E.1    Nakai, S.2    Wood, D.3
  • 20
    • 18744369369 scopus 로고    scopus 로고
    • cDNA cloning of myosin heavy chain from white croacker fast skeletal muscle and characterization of its complete primary structure.
    • Yoon S. H., Kakimuma M., Hirayama Y., Yamamoto T., Watabe S. cDNA cloning of myosin heavy chain from white croacker fast skeletal muscle and characterization of its complete primary structure. Fisheries Sci. 2000; 66: 1163–1171.
    • (2000) Fisheries Sci. , vol.66 , pp. 1163-1171
    • Yoon, S.H.1    Kakimuma, M.2    Hirayama, Y.3    Yamamoto, T.4    Watabe, S.5
  • 21
    • 0001136664 scopus 로고    scopus 로고
    • cDNA cloning of myosin rod and the complete primary structure of myosin heavy chain of walleye pollack fast skeletal muscle.
    • Togashi M., Kakinuma M., Hirayama Y., Fukushima H., Watabe S., Ojima T., Nishita, K. cDNA cloning of myosin rod and the complete primary structure of myosin heavy chain of walleye pollack fast skeletal muscle. Fisheries Sci. 2000; 66: 349–357.
    • (2000) Fisheries Sci. , vol.66 , pp. 349-357
    • Togashi, M.1    Kakinuma, M.2    Hirayama, Y.3    Fukushima, H.4    Watabe, S.5    Ojima, T.6    Nishita, K.7
  • 22
    • 0023658390 scopus 로고
    • Characterzation of cDNA coding for the complete light meromyosin portion of a rabbit fast skeletal muscle myosin heavy chain.
    • Maeda K., Sczakiel G., Wittinghofer A. Characterzation of cDNA coding for the complete light meromyosin portion of a rabbit fast skeletal muscle myosin heavy chain. Eur. J. Biochem. 1987; 167: 97–102.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 97-102
    • Maeda, K.1    Sczakiel, G.2    Wittinghofer, A.3
  • 23
    • 0025779542 scopus 로고
    • Expression in Escherichia coli of fragments of the coiled-coil rod domain of rabbit myosin: influence of different regions of the molecule on aggregation and paracrystal formation.
    • Atkinson S. J., Stewart M. Expression in Escherichia coli of fragments of the coiled-coil rod domain of rabbit myosin: influence of different regions of the molecule on aggregation and paracrystal formation. J. Cell Sci. 1991; 99: 823–836.
    • (1991) J. Cell Sci. , vol.99 , pp. 823-836
    • Atkinson, S.J.1    Stewart, M.2
  • 25
    • 0009927045 scopus 로고    scopus 로고
    • Thermal unfolding of the cold-acclimated type of carp light meromyosin expressed by recombinant DNA in Escherichia coli.
    • Kakinuma M., Funabara D., Nakaya M., Hirayama Y., Watabe S., Maeda K., Ooi T. Thermal unfolding of the cold-acclimated type of carp light meromyosin expressed by recombinant DNA in Escherichia coli. Fisheries Sci. 1997; 63: 1008–1013.
    • (1997) Fisheries Sci. , vol.63 , pp. 1008-1013
    • Kakinuma, M.1    Funabara, D.2    Nakaya, M.3    Hirayama, Y.4    Watabe, S.5    Maeda, K.6    Ooi, T.7
  • 26
    • 0032485915 scopus 로고    scopus 로고
    • Thermal unfolding of three acclimation temperature-associated isoforms of carp light meromyosin expressed by recombinant DNAs
    • Kakinuma M., Nakaya M., Hatanaka A., Hirayama Y., Watabe S., Maeda K., Ooi T., Suzuki S. Thermal unfolding of three acclimation temperature-associated isoforms of carp light meromyosin expressed by recombinant DNAs. Biochemistry 1998; 37: 6606–6613.
    • (1998) Biochemistry , vol.37 , pp. 6606-6613
    • Kakinuma, M.1    Nakaya, M.2    Hatanaka, A.3    Hirayama, Y.4    Watabe, S.5    Maeda, K.6    Ooi, T.7    Suzuki, S.8
  • 27
    • 0033930401 scopus 로고    scopus 로고
    • Differential scanning calorimetry of light meromyosin fragments having various lengths of carp fast skeletal muscle isoforms.
    • Kakinuma M., Hatanaka A., Fukushima H., Nakaya M., Maeda K., Doi Y., Ooi T., Watabe S. Differential scanning calorimetry of light meromyosin fragments having various lengths of carp fast skeletal muscle isoforms. J. Biochem. 2000; 128: 11–20.
    • (2000) J. Biochem. , vol.128 , pp. 11-20
    • Kakinuma, M.1    Hatanaka, A.2    Fukushima, H.3    Nakaya, M.4    Maeda, K.5    Doi, Y.6    Ooi, T.7    Watabe, S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.