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Volumn 76, Issue 7, 2011, Pages

Thermophysical Characterization of Tilapia Myosin and Its Subfragments

Author keywords

HMM; LMM; Myosin; Thermophysical; Tilapia

Indexed keywords

ALPHA-CHYMOTRYPSIN; CHYMOTRYPSIN; CHYMOTRYPSIN A; MYOSIN; MYOSIN SUBFRAGMENT;

EID: 80053069256     PISSN: 00221147     EISSN: 17503841     Source Type: Journal    
DOI: 10.1111/j.1750-3841.2011.02330.x     Document Type: Article
Times cited : (29)

References (34)
  • 1
    • 0000827266 scopus 로고
    • Thermal aggregation of myosin subfragments from cod and herring
    • Chan JK, Gill TA, Paulson AT. 1993. Thermal aggregation of myosin subfragments from cod and herring. J Food Sci 58(5):1057-61.
    • (1993) J Food Sci , vol.58 , Issue.5 , pp. 1057-1061
    • Chan, J.K.1    Gill, T.A.2    Paulson, A.T.3
  • 2
    • 84982335313 scopus 로고
    • Changes in amount of myosin extractable from cod flesh during storage at -14°C
    • November):-
    • Connell JJ. 1962. Changes in amount of myosin extractable from cod flesh during storage at -14°C. J Sci Food Agric 13(November):607-17.
    • (1962) J Sci Food Agric , vol.13 , pp. 607-617
    • Connell, J.J.1
  • 4
    • 0023993757 scopus 로고
    • Extension of a model for crosslinking polymer at the gel point
    • Friedrich C, Heymann L. 1988. Extension of a model for crosslinking polymer at the gel point. J Rheol 32(3):235-41.
    • (1988) J Rheol , vol.32 , Issue.3 , pp. 235-241
    • Friedrich, C.1    Heymann, L.2
  • 5
    • 0002832945 scopus 로고
    • Effect of salt concentration and temperature on heat-induced aggregation and gelation of fish myosin
    • Gill TA, Chan JK, Phonchareon KF, Paulson AT. 1992. Effect of salt concentration and temperature on heat-induced aggregation and gelation of fish myosin. Food Res Int 25(5):333-41.
    • (1992) Food Res Int , vol.25 , Issue.5 , pp. 333-341
    • Gill, T.A.1    Chan, J.K.2    Phonchareon, K.F.3    Paulson, A.T.4
  • 6
    • 10944231111 scopus 로고    scopus 로고
    • The tail of myosin reduces actin filament velocity in thein vitromotility assay
    • Guo B, Guilford W. 2004. The tail of myosin reduces actin filament velocity in thein vitromotility assay. Cell Motil Cytoskel 59(4):264-72.
    • (2004) Cell Motil Cytoskel , vol.59 , Issue.4 , pp. 264-272
    • Guo, B.1    Guilford, W.2
  • 7
    • 0033766762 scopus 로고    scopus 로고
    • A myosin family tree
    • Hodge T, Cope M. 2000. A myosin family tree. J Cell Sci 113(Pt 19):3353-54.
    • (2000) J Cell Sci , vol.113 , Issue.PART 19 , pp. 3353-3354
    • Hodge, T.1    Cope, M.2
  • 8
    • 80053062808 scopus 로고    scopus 로고
    • In: Coluccio L, editor. Myosins Dordrecht, Netherlands Springer.
    • Holmes K. 2008. Myosin structure. In: Coluccio L, editor. Myosins Dordrecht, Netherlands Springer. p. 1-34.
    • (2008) Myosin structure. , pp. 1-34
    • Holmes, K.1
  • 9
    • 69349086645 scopus 로고    scopus 로고
    • Gelation of protein isolates extracted from tilapia light muscle by pH shift processing
    • Ingadottir B, Kristinsson HG. 2010. Gelation of protein isolates extracted from tilapia light muscle by pH shift processing. Food Chem 118(3):789-98.
    • (2010) Food Chem , vol.118 , Issue.3 , pp. 789-798
    • Ingadottir, B.1    Kristinsson, H.G.2
  • 10
    • 26844557071 scopus 로고    scopus 로고
    • Gel forming ability of tropical tilapia surimi as compared with Alaska pollock and Pacific whiting surimi
    • Klesk K, Yongsawatdigul J, Park JW, Viratchakul S, Virulhakul P. 2000. Gel forming ability of tropical tilapia surimi as compared with Alaska pollock and Pacific whiting surimi. J Aqua Food Prod Technol 9(3):91-104.
    • (2000) J Aqua Food Prod Technol , vol.9 , Issue.3 , pp. 91-104
    • Klesk, K.1    Yongsawatdigul, J.2    Park, J.W.3    Viratchakul, S.4    Virulhakul, P.5
  • 11
    • 33748339636 scopus 로고    scopus 로고
    • Surimi gelation chemistry
    • In: Park JW, editor. 2nd ed. Boca Raton, Fla. CRC Press Taylor & Francis Group.
    • Lanier TC, Carvajal P, Yongsawatdigul J. 2005. Surimi gelation chemistry. In: Park JW, editor. Surimi and surimi seafood. 2nd ed. Boca Raton, Fla. CRC Press Taylor & Francis Group. p. 435-89.
    • (2005) Surimi and surimi seafood , pp. 435-489
    • Lanier, T.C.1    Carvajal, P.2    Yongsawatdigul, J.3
  • 13
    • 84912490374 scopus 로고
    • Studies on the structure of myosin
    • IN215-IN217.
    • Lowey S, Cohen C. 1962. Studies on the structure of myosin. J Mol Biol 4(4):293-308, IN215-IN217.
    • (1962) J Mol Biol , vol.4 , Issue.4 , pp. 293-308
    • Lowey, S.1    Cohen, C.2
  • 14
    • 0014693726 scopus 로고
    • Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation
    • Lowey S, Slayter H, Weeds A, Baker H. 1969. Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation. J Mol Biol 42(1):1-29.
    • (1969) J Mol Biol , vol.42 , Issue.1 , pp. 1-29
    • Lowey, S.1    Slayter, H.2    Weeds, A.3    Baker, H.4
  • 15
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian S, Lowey S. 1982. Preparation of myosin and its subfragments from rabbit skeletal muscle. Method Enzymol 85:55-71.
    • (1982) Method Enzymol , vol.85 , pp. 55-71
    • Margossian, S.1    Lowey, S.2
  • 16
    • 0007285616 scopus 로고
    • A simplified myosin preparation from marine fish species
    • Martone C, Busconi L, Folco E, Trucco R, Sanchez J. 1986. A simplified myosin preparation from marine fish species. J Food Sci 51(6):1554-5.
    • (1986) J Food Sci , vol.51 , Issue.6 , pp. 1554-1555
    • Martone, C.1    Busconi, L.2    Folco, E.3    Trucco, R.4    Sanchez, J.5
  • 18
    • 0032696893 scopus 로고    scopus 로고
    • Properties of myofibrillar protein from Japanese stingfish (Sebastes inermis) dorsal muscle
    • Nagai T, Kurata M, Nakamura T, Ito T, Fujiki K, Nakao M, Yano T. 1999. Properties of myofibrillar protein from Japanese stingfish (Sebastes inermis) dorsal muscle. Food Res Int 32(6):401-5.
    • (1999) Food Res Int , vol.32 , Issue.6 , pp. 401-405
    • Nagai, T.1    Kurata, M.2    Nakamura, T.3    Ito, T.4    Fujiki, K.5    Nakao, M.6    Yano, T.7
  • 19
    • 0030857497 scopus 로고    scopus 로고
    • Differential scanning calorimetry and CD spectrometry of acclimation temperature-associated types of carp light meromyosin
    • Nakaya M, Kakinuma M, Watabe S, Ooi T. 1997. Differential scanning calorimetry and CD spectrometry of acclimation temperature-associated types of carp light meromyosin. Biochemistry 36(30):9179-84.
    • (1997) Biochemistry , vol.36 , Issue.30 , pp. 9179-9184
    • Nakaya, M.1    Kakinuma, M.2    Watabe, S.3    Ooi, T.4
  • 20
    • 0028913571 scopus 로고    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. 2002. Differences in the thermal stability of acclimation temperature-associated types of carp myosin and its rod on differential scanning calorimetry. Biochemistry 34(9):3114-20.
    • (2002) Biochemistry , vol.34 , Issue.9 , pp. 3114-3120
    • Nakaya, M.1    Watabe, S.2    Ooi, T.3
  • 21
    • 0032930419 scopus 로고    scopus 로고
    • Comparison of the stability of fish light meromyosins by guanidine hydrochloride denaturation
    • Ogawa M, Miyagi R, Tamiya T, Tsuchiya T. 1999. Comparison of the stability of fish light meromyosins by guanidine hydrochloride denaturation. Comp Biochem Phys B 122B(4):439-46.
    • (1999) Comp Biochem Phys B , vol.122 , Issue.4 , pp. 439-446
    • Ogawa, M.1    Miyagi, R.2    Tamiya, T.3    Tsuchiya, T.4
  • 22
    • 84985181056 scopus 로고
    • Calorimetric changes during development of rigor mortis
    • Park J, Lanier T. 1988. Calorimetric changes during development of rigor mortis. J Food Sci 53(5):1312-72.
    • (1988) J Food Sci , vol.53 , Issue.5 , pp. 1312-1372
    • Park, J.1    Lanier, T.2
  • 23
    • 33748376956 scopus 로고    scopus 로고
    • Surimi seafood: products, market, and manufacturing
    • In: Park JW, editor. 2nd ed. Boca Raton, Fla. CRC Press Taylor & Francis Group.
    • Park JW. 2005. Surimi seafood: products, market, and manufacturing. In: Park JW, editor. Surimi and surimi seafood. 2nd ed. Boca Raton, Fla. CRC Press Taylor & Francis Group. p. 375-433.
    • (2005) Surimi and surimi seafood , pp. 375-433
    • Park, J.W.1
  • 24
    • 80053067801 scopus 로고    scopus 로고
    • Thermal denaturation of tilapia myosin, heavy meromyosin, and light meromyosin as affected by a constantly increasing temperature
    • Reed ZH, Guilford W, Park JW. 2011. Thermal denaturation of tilapia myosin, heavy meromyosin, and light meromyosin as affected by a constantly increasing temperature. J Food Sci 76(7):C1018-1024.
    • (2011) J Food Sci , vol.76 , Issue.7
    • Reed, Z.H.1    Guilford, W.2    Park, J.W.3
  • 25
    • 84987300642 scopus 로고
    • Thermal gelation characteristics of myosin subfragments
    • Sano T, Noguchi S, Matsumoto J, Tsuchiya T. 1990. Thermal gelation characteristics of myosin subfragments. J Food Sci 55(1):55-8.
    • (1990) J Food Sci , vol.55 , Issue.1 , pp. 55-58
    • Sano, T.1    Noguchi, S.2    Matsumoto, J.3    Tsuchiya, T.4
  • 26
    • 33645328300 scopus 로고    scopus 로고
    • Role of cooling process in the thermal aggregate formation by carp myosin rod
    • Sasaki T, Yuan C, Konno K. 2006. Role of cooling process in the thermal aggregate formation by carp myosin rod. J Food Sci 71(2):C75-C80.
    • (2006) J Food Sci , vol.71 , Issue.2
    • Sasaki, T.1    Yuan, C.2    Konno, K.3
  • 27
    • 0025321594 scopus 로고
    • Differential scanning calorimetry of the unfolding of myosin subfragment 1, subfragment 2, and heavy meromyosin
    • Shriver JW, Kamath U. 1990. Differential scanning calorimetry of the unfolding of myosin subfragment 1, subfragment 2, and heavy meromyosin. Biochemistry 29(10):2556-64.
    • (1990) Biochemistry , vol.29 , Issue.10 , pp. 2556-2564
    • Shriver, J.W.1    Kamath, U.2
  • 28
    • 0000668251 scopus 로고
    • Meromyosins: the subunits of myosin
    • Szent-Görgyi AG. 1953. Meromyosins: the subunits of myosin. Arch Biochem Biophys 42:305-20.
    • (1953) Arch Biochem Biophys , vol.42 , pp. 305-320
    • Szent-Görgyi, A.G.1
  • 29
    • 0037077363 scopus 로고    scopus 로고
    • Differential scanning calorimetry and circular dichroism spectrometry of walleye pollack myosin and light meromyosin
    • Togashi M, Kakinuma M, Nayaka M, Ooi T, Watabe S. 2002. Differential scanning calorimetry and circular dichroism spectrometry of walleye pollack myosin and light meromyosin. J Agric Food Chem 50(17):4803-11.
    • (2002) J Agric Food Chem , vol.50 , Issue.17 , pp. 4803-4811
    • Togashi, M.1    Kakinuma, M.2    Nayaka, M.3    Ooi, T.4    Watabe, S.5
  • 31
    • 0010563775 scopus 로고
    • Isolation, purification and structure of carp myosin, HMM and LMM
    • Tsuchiya T, Matsumoto J. 1975. Isolation, purification and structure of carp myosin, HMM and LMM. Bull Jap Sc Sci Fish 42(12):1319-26.
    • (1975) Bull Jap Sc Sci Fish , vol.42 , Issue.12 , pp. 1319-1326
    • Tsuchiya, T.1    Matsumoto, J.2
  • 32
    • 84989743963 scopus 로고
    • Can the gel point of a cross-linking polymer be detected by the G'- G" crossover
    • Winter HH. 1987. Can the gel point of a cross-linking polymer be detected by the G'- G" crossover Polym Eng Sci 27(22):1698-02.
    • (1987) Polym Eng Sci , vol.27 , Issue.22 , pp. 1698-1602
    • Winter, H.H.1
  • 33
    • 0022694827 scopus 로고
    • Analysis of linear viscoelasticity of a crosslinking polymer at the gel point
    • Winter HH, Chambon F. 1986. Analysis of linear viscoelasticity of a crosslinking polymer at the gel point. J Rheol 30(2):367-82.
    • (1986) J Rheol , vol.30 , Issue.2 , pp. 367-382
    • Winter, H.H.1    Chambon, F.2
  • 34
    • 0032867089 scopus 로고    scopus 로고
    • Thermal aggregation and dynamic rheological properties of Pacific whiting and cod myosins as affected by heating rate
    • Yongsawatdigul J, Park JW. 1999. Thermal aggregation and dynamic rheological properties of Pacific whiting and cod myosins as affected by heating rate. J Food Sci 64(4):679-83.
    • (1999) J Food Sci , vol.64 , Issue.4 , pp. 679-683
    • Yongsawatdigul, J.1    Park, J.W.2


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