메뉴 건너뛰기




Volumn 70, Issue 8, 2005, Pages

Ca2+ affects physicochemical and conformational changes of threadfin bream myosin and actin in a setting model

Author keywords

Actin; Calcium; Myosin; Setting; Threadfin bream

Indexed keywords

NEMIPTERIDAE;

EID: 27544442211     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2005.tb11500.x     Document Type: Article
Times cited : (48)

References (32)
  • 1
    • 0021755248 scopus 로고
    • Mechanism of protein salting in and salting out by divalent cation salts: Balance between hydration and salt binding
    • Arakawa T, Timasheff SN. 1984. Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding. Biochem 23:5912-23.
    • (1984) Biochem , vol.23 , pp. 5912-5923
    • Arakawa, T.1    Timasheff, S.N.2
  • 2
    • 0029792830 scopus 로고    scopus 로고
    • How hofmeister ion interactions affect protein stability
    • Baldwin R. 1996. How hofmeister ion interactions affect protein stability. Biophys J 71:2056-63.
    • (1996) Biophys J , vol.71 , pp. 2056-2063
    • Baldwin, R.1
  • 3
    • 0024351996 scopus 로고
    • Correlation among the proton charges and molecular masses of myosin subunits
    • Bechet JJ, Albis A. 1989. Correlation among the proton charges and molecular masses of myosin subunits. FEBS Lett 249:8-12.
    • (1989) FEBS Lett , vol.249 , pp. 8-12
    • Bechet, J.J.1    Albis, A.2
  • 4
    • 0242490912 scopus 로고    scopus 로고
    • Suwari gel properties as affected by transglutaminase activator and inhibitors
    • Benjakul S, Visessanguan W, Pecharat, S. 2004. Suwari gel properties as affected by transglutaminase activator and inhibitors. Food Chem 85:91-9.
    • (2004) Food Chem , vol.85 , pp. 91-99
    • Benjakul, S.1    Visessanguan, W.2    Pecharat, S.3
  • 5
    • 0017184389 scopus 로고
    • A rapid sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M. 1976. A rapid sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72:248-52.
    • (1976) Anal Biochem , vol.72 , pp. 248-252
    • Bradford, M.1
  • 6
    • 84986505834 scopus 로고
    • Herring surimi during low temperature setting, physicochemical and textural properties
    • Chan JK, Gill TA, Thompson JW, Singer DS. 1995. Herring surimi during low temperature setting, physicochemical and textural properties. J Food Sci 60:1248-53.
    • (1995) J Food Sci , vol.60 , pp. 1248-1253
    • Chan, J.K.1    Gill, T.A.2    Thompson, J.W.3    Singer, D.S.4
  • 7
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman GL. 1959. Tissue sulfhydryl groups. Arch Biochem Biophys 82:70-7.
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 8
    • 0018816617 scopus 로고
    • Transglutaminase
    • Folk JE. 1980. Transglutaminase. Ann Rev Biochem 49:517-31.
    • (1980) Ann Rev Biochem , vol.49 , pp. 517-531
    • Folk, J.E.1
  • 9
    • 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 25:333-41.
    • (1992) Food Res Int , vol.25 , pp. 333-341
    • Gill, T.A.1    Chan, J.K.2    Phonchareon, K.F.3    Paulson, A.T.4
  • 10
    • 0002593957 scopus 로고
    • Calcium binding and salt-induced structural changes of native and preheated β-lactoglobulin
    • Jeyarajah S, Allen JC. 1994. Calcium binding and salt-induced structural changes of native and preheated β-lactoglobulin. J Agric Food Chem 42:80-5.
    • (1994) J Agric Food Chem , vol.42 , pp. 80-85
    • Jeyarajah, S.1    Allen, J.C.2
  • 11
    • 84986522949 scopus 로고
    • Nondisulfide covalent cross-linking of myosin heavy chain in "setting" of Alaska pollock and Atlantic croaker surimi
    • Kamath GG, Lanier TC, Foegeding EA, Hamann DD. 1992. Nondisulfide covalent cross-linking of myosin heavy chain in "setting" of Alaska pollock and Atlantic croaker surimi. J Food Biochem 16:151-72.
    • (1992) J Food Biochem , vol.16 , pp. 151-172
    • Kamath, G.G.1    Lanier, T.C.2    Foegeding, E.A.3    Hamann, D.D.4
  • 12
    • 0012165312 scopus 로고    scopus 로고
    • Physical behavior of tilapia (Oreochromis niloticus) surimi gels at various thermal treatments as compared with Alaska pollock and Pacific whiting surimi
    • Klesk K, Yongsawatdigul J, Park JW, Viratchakul S, Virulhakul P. 2000. Physical behavior of tilapia (Oreochromis niloticus) surimi gels at various thermal treatments as compared with Alaska pollock and Pacific whiting surimi. J Aquat Food Prod Tech 9:91-104.
    • (2000) J Aquat Food Prod Tech , vol.9 , pp. 91-104
    • Klesk, K.1    Yongsawatdigul, J.2    Park, J.W.3    Viratchakul, S.4    Virulhakul, P.5
  • 13
    • 0001522023 scopus 로고
    • Suppression of surimi gel setting by transglutaminase inhibitors
    • Kumazawa Y, Numazawa T, Seguro K, Motoki M. 1995. Suppression of surimi gel setting by transglutaminase inhibitors. J Food Sci 60:715-7.
    • (1995) J Food Sci , vol.60 , pp. 715-717
    • Kumazawa, Y.1    Numazawa, T.2    Seguro, K.3    Motoki, M.4
  • 14
    • 0001554239 scopus 로고    scopus 로고
    • Surimi gelation chemistry
    • Park JW, editor. New York: Marcel Dekker
    • Lanier TC. 2000. Surimi gelation chemistry. In: Park JW, editor. Surimi and surimi seafood. New York: Marcel Dekker. p 237-65.
    • (2000) Surimi and Surimi Seafood , pp. 237-265
    • Lanier, T.C.1
  • 15
    • 0032416267 scopus 로고    scopus 로고
    • Calcium compounds to improve gel functionality of Pacific whiting and Alaska pollock surimi
    • Lee N, Park JW. 1998. Calcium compounds to improve gel functionality of Pacific whiting and Alaska pollock surimi. J Food Sci 63:969-74.
    • (1998) J Food Sci , vol.63 , pp. 969-974
    • Lee, N.1    Park, J.W.2
  • 16
    • 0015526770 scopus 로고
    • Intrinsic fluorescence of actin
    • Lehrer SS, Kerwar G. 1972. Intrinsic fluorescence of actin. Biochemistry 11:1211-7.
    • (1972) Biochemistry , vol.11 , pp. 1211-1217
    • Lehrer, S.S.1    Kerwar, G.2
  • 17
    • 84986736089 scopus 로고
    • Relationship between functional (fat binding, emulsifying) and physicochemical properties of muscle protiens. Effects of heating, freezing, pH, and species
    • Li-Chan E, Nakai S, Wood DF. 1985. Relationship between functional (fat binding, emulsifying) and physicochemical properties of muscle protiens. Effects of heating, freezing, pH, and species. J Food Sci 50:1034-40.
    • (1985) J Food Sci , vol.50 , pp. 1034-1040
    • Li-Chan, E.1    Nakai, S.2    Wood, D.F.3
  • 19
    • 84985233021 scopus 로고
    • Actomyosin stabilitzation to freeze-thaw and heat denaturation by Lactate salts
    • MacDonald GA, Lanier TC. 1994. Actomyosin stabilitzation to freeze-thaw and heat denaturation by Lactate salts. J Food Sci 59:101-5.
    • (1994) J Food Sci , vol.59 , pp. 101-105
    • MacDonald, G.A.1    Lanier, T.C.2
  • 22
    • 0015359461 scopus 로고
    • Optical rotatory dispersion and circular dichroic spectra of G-actin
    • Nagy B, Goaszewska HS. 1972. Optical rotatory dispersion and circular dichroic spectra of G-actin. Arch Biochem Biophy 150:428-35.
    • (1972) Arch Biochem Biophy , vol.150 , pp. 428-435
    • Nagy, B.1    Goaszewska, H.S.2
  • 24
  • 27
    • 0000252971 scopus 로고
    • On the solubility of cod muscle proteins in water
    • Stefansson C, Hultin HO. 1994. On the solubility of cod muscle proteins in water. J Agric Food Chem 42:2656-64.
    • (1994) J Agric Food Chem , vol.42 , pp. 2656-2664
    • Stefansson, C.1    Hultin, H.O.2
  • 28
    • 0001148024 scopus 로고
    • The solubilization of myofibrillar proteins by calcium ions
    • Taylor M, Etherington DJ. 1991. The solubilization of myofibrillar proteins by calcium ions. Meat Sci 29:211-9.
    • (1991) Meat Sci , vol.29 , pp. 211-219
    • Taylor, M.1    Etherington, D.J.2
  • 30
    • 0037137137 scopus 로고    scopus 로고
    • Calcium-induced decrease of the thermal stability and chaperone activity of α-crystalline
    • Valle LJ, Escribano C, Perez JJ, Garriga P. 2002. Calcium-induced decrease of the thermal stability and chaperone activity of α-crystalline. Biochem Biophys Acta 1601:100-9.
    • (2002) Biochem Biophys Acta , vol.1601 , pp. 100-109
    • Valle, L.J.1    Escribano, C.2    Perez, J.J.3    Garriga, P.4
  • 31
    • 0036868154 scopus 로고    scopus 로고
    • Effect of endogenous transglutaminase on threadfin bream surimi gelation
    • Yongsawatdigul J, Worratao A, Park JW. 2002. Effect of endogenous transglutaminase on threadfin bream surimi gelation. J Food Sci 67:3258-63.
    • (2002) J Food Sci , vol.67 , pp. 3258-3263
    • Yongsawatdigul, J.1    Worratao, A.2    Park, J.W.3
  • 32
    • 0041386023 scopus 로고    scopus 로고
    • Thermal denaturation and aggregation of threadfin bream actomyosin
    • Yongsawatdigul J, Park JW. 2003. Thermal denaturation and aggregation of threadfin bream actomyosin. Food Chem 83:409-16.
    • (2003) Food Chem , vol.83 , pp. 409-416
    • Yongsawatdigul, J.1    Park, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.