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Volumn 55, Issue 10, 2007, Pages 4144-4153

Conformational and rheological changes in catfish myosin as affected by different acids during acid-induced unfolding and refolding

Author keywords

Acid unfolding; Anion; Catfish; Conformation; Gelation; Myosin; pH; pH shift; Salt

Indexed keywords

MYOSIN;

EID: 34249865663     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf063184v     Document Type: Conference Paper
Times cited : (28)

References (34)
  • 1
    • 0028311361 scopus 로고
    • Myofibrillar protein from different muscle-fiber types - Implications of biochemical and functional-properties in meat processing
    • Xiong, Y. L. L. Myofibrillar protein from different muscle-fiber types - Implications of biochemical and functional-properties in meat processing. Crit. Rev. Food Sci. Nutr. 1994, 34 (3), 293-320.
    • (1994) Crit. Rev. Food Sci. Nutr , vol.34 , Issue.3 , pp. 293-320
    • Xiong, Y.L.L.1
  • 2
    • 0021782026 scopus 로고
    • Functionality of muscle proteins in gelation mechanisms of structured meat-products
    • Asghar, A.; Samejima, K.; Yasui, T. Functionality of muscle proteins in gelation mechanisms of structured meat-products. CRC Crit. Rev. Food Sci. Nutr. 1985, 22 (1), 27-106.
    • (1985) CRC Crit. Rev. Food Sci. Nutr , vol.22 , Issue.1 , pp. 27-106
    • Asghar, A.1    Samejima, K.2    Yasui, T.3
  • 3
    • 0012165343 scopus 로고    scopus 로고
    • Process for isolating a protein composition from a muscle source and protein composition
    • U.S. Patent 6005073
    • Hultin, H. O.; Kelleher, S. D. Process for isolating a protein composition from a muscle source and protein composition. U.S. Patent 6005073, 1999.
    • (1999)
    • Hultin, H.O.1    Kelleher, S.D.2
  • 4
    • 0002454157 scopus 로고    scopus 로고
    • Surimi processing from dark muscle fish
    • Park, J. W, Ed, Marcel Dekker: New York
    • Hultin, H. O.; Kelleher, S. D. Surimi processing from dark muscle fish. In Surimi and Surimi Seafood; Park, J. W., Ed.; Marcel Dekker: New York, 2000; pp 59-78.
    • (2000) Surimi and Surimi Seafood , pp. 59-78
    • Hultin, H.O.1    Kelleher, S.D.2
  • 5
    • 0034091953 scopus 로고    scopus 로고
    • Effects of proteolysis and mechanism of gel weakening in heat-induced gelation of fish myosin
    • Visessanguan, W.; An, H. Effects of proteolysis and mechanism of gel weakening in heat-induced gelation of fish myosin. J. Agric. Food Chem. 2000, 48 (4), 1024-1032.
    • (2000) J. Agric. Food Chem , vol.48 , Issue.4 , pp. 1024-1032
    • Visessanguan, W.1    An, H.2
  • 6
    • 0030694792 scopus 로고    scopus 로고
    • Solubilization of fish muscle myosin by sorbitol
    • Konno, K.; Yamanodera, K.; Kiuchi, H. Solubilization of fish muscle myosin by sorbitol. J. Food Sci. 1997, 62 (5), 980-984.
    • (1997) J. Food Sci , vol.62 , Issue.5 , pp. 980-984
    • Konno, K.1    Yamanodera, K.2    Kiuchi, H.3
  • 7
    • 0001954905 scopus 로고    scopus 로고
    • Functional chicken muscle protein isolates prepared using low ionic strength, acid solubilizatiion/ precipitation
    • Kelleher, S. D.; Hultin, H. O. Functional chicken muscle protein isolates prepared using low ionic strength, acid solubilizatiion/ precipitation. Reciprocal Meat Conf. Proc 2000, 76-81.
    • (2000) Reciprocal Meat Conf. Proc , pp. 76-81
    • Kelleher, S.D.1    Hultin, H.O.2
  • 9
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto, Y.; Takahashi, N.; Fink, A. L. Mechanism of acid-induced folding of proteins. Biochemistry 1990, 29 (14), 3480-3488.
    • (1990) Biochemistry , vol.29 , Issue.14 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.L.3
  • 10
    • 0030727624 scopus 로고    scopus 로고
    • The Hofmeister series: Salt and solvent effects on interfacial phenomena
    • Cacace, M. G.; Landau, E. M.; Ramsden, J. J. The Hofmeister series: Salt and solvent effects on interfacial phenomena. Q. Rev. Biophys. 1997, 30 (3), 241-277.
    • (1997) Q. Rev. Biophys , vol.30 , Issue.3 , pp. 241-277
    • Cacace, M.G.1    Landau, E.M.2    Ramsden, J.J.3
  • 11
    • 1942521068 scopus 로고    scopus 로고
    • Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins
    • Arakawa, T.; Tokunaga, M. Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins. Protein Pept. Lett. 2004, 11 (2), 125-132.
    • (2004) Protein Pept. Lett , vol.11 , Issue.2 , pp. 125-132
    • Arakawa, T.1    Tokunaga, M.2
  • 12
    • 0017623134 scopus 로고
    • Salt effects on hydrophobic interactions in precipitation and chromatography of proteins - Interpretation of lyotropic series
    • Melander, W.; Horvath, C. Salt effects on hydrophobic interactions in precipitation and chromatography of proteins - Interpretation of lyotropic series. Arch. Biochem. Biophys. 1977, 183 (1), 200-215.
    • (1977) Arch. Biochem. Biophys , vol.183 , Issue.1 , pp. 200-215
    • Melander, W.1    Horvath, C.2
  • 13
    • 0035533232 scopus 로고    scopus 로고
    • Evaluation of different methods to isolate cod (Gadus morhua) muscle myosin
    • Kristinsson, H. G. Evaluation of different methods to isolate cod (Gadus morhua) muscle myosin. J. Food Biochem. 2001, 25 (3), 249-256.
    • (2001) J. Food Biochem , vol.25 , Issue.3 , pp. 249-256
    • Kristinsson, H.G.1
  • 14
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornali, A. G.; Bardawill, C. J.; David, M. M. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 1949, 177 (2), 751-766.
    • (1949) J. Biol. Chem , vol.177 , Issue.2 , pp. 751-766
    • Gornali, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 15
    • 0018786922 scopus 로고    scopus 로고
    • Weber, G.; Farris, F. J. Synthesis and spectral properties of a hydrophobic fluorescent-probe - 6-Propionyl-2-(dimethylamino) naphthalene. Biochemistry 1979, 18 (14), 3075-3078.
    • Weber, G.; Farris, F. J. Synthesis and spectral properties of a hydrophobic fluorescent-probe - 6-Propionyl-2-(dimethylamino) naphthalene. Biochemistry 1979, 18 (14), 3075-3078.
  • 16
    • 0036168995 scopus 로고    scopus 로고
    • An interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • Lobley, A.; Whitmore, L.; Wallace, B. A. DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 2002, 18 (1), 211-212.
    • (2002) Bioinformatics , vol.18 , Issue.1 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.3    DICHROWEB, A.4
  • 17
    • 0000922902 scopus 로고
    • Studies on the proteins of fish skeletal muscle. 7. Denaturation and aggregation of cod myosin
    • Connell, J. J. Studies on the proteins of fish skeletal muscle. 7. Denaturation and aggregation of cod myosin. Biochem. J. 1960, 75, 530-538.
    • (1960) Biochem. J , vol.75 , pp. 530-538
    • Connell, J.J.1
  • 19
    • 0033629370 scopus 로고    scopus 로고
    • Denaturation of myofibrillar proteins from chickens as affected by pH, temperature, and adenosine triphosphate concentration
    • Van Laack, R. L.; Lane, J. L. Denaturation of myofibrillar proteins from chickens as affected by pH, temperature, and adenosine triphosphate concentration. Poult. Sci. 2000, 79 (1), 105-109.
    • (2000) Poult. Sci , vol.79 , Issue.1 , pp. 105-109
    • Van Laack, R.L.1    Lane, J.L.2
  • 20
    • 0039890179 scopus 로고    scopus 로고
    • Effect of pH on the gelation of walleye pollack surimi and carp actomyosin pastes
    • Ni, S. W.; Nozawa, H.; Seki, N. Effect of pH on the gelation of walleye pollack surimi and carp actomyosin pastes. Fish. Sci. 2001, 67 (5), 920-927.
    • (2001) Fish. Sci , vol.67 , Issue.5 , pp. 920-927
    • Ni, S.W.1    Nozawa, H.2    Seki, N.3
  • 21
    • 0042061104 scopus 로고    scopus 로고
    • Effect of low and high pH treatment on the functional properties of cod muscle proteins
    • Kristinsson, H. G.; Hultin, H. O. Effect of low and high pH treatment on the functional properties of cod muscle proteins. J. Agric. Food. Chem. 2003, 51 (17), 5103-5110.
    • (2003) J. Agric. Food. Chem , vol.51 , Issue.17 , pp. 5103-5110
    • Kristinsson, H.G.1    Hultin, H.O.2
  • 22
    • 0002125934 scopus 로고
    • The Mechanism of formation of gels from myosin molecules
    • Sharp, A.; Offer, G. The Mechanism of formation of gels from myosin molecules. J. Sci. Food Agric. 1992, 58 (1), 63-73.
    • (1992) J. Sci. Food Agric , vol.58 , Issue.1 , pp. 63-73
    • Sharp, A.1    Offer, G.2
  • 23
    • 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 (5), 1412-1418.
    • (1981) J. Food Sci , vol.46 , Issue.5 , pp. 1412-1418
    • Samejima, K.1    Ishioroshi, M.2    Yasui, T.3
  • 24
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. Dominant forces in protein folding. Biochemistry 1990, 29 (31), 7133-7155.
    • (1990) Biochemistry , vol.29 , Issue.31 , pp. 7133-7155
    • Dill, K.A.1
  • 25
    • 0037077363 scopus 로고    scopus 로고
    • Differential scanning calorimetry and circular dichroism spectrometry of walleye pollack myosin and light meromyosin
    • Togashi, M.; Kakinuma, M.; Nakaya, M.; Ooi, T.; Watabe, S. Differential scanning calorimetry and circular dichroism spectrometry of walleye pollack myosin and light meromyosin. J. Agric Food. Chem. 2002, 50 (17), 4803-4811.
    • (2002) J. Agric Food. Chem , vol.50 , Issue.17 , pp. 4803-4811
    • Togashi, M.1    Kakinuma, M.2    Nakaya, M.3    Ooi, T.4    Watabe, S.5
  • 27
    • 84985266593 scopus 로고
    • Hydrophobicity and solubility of meat proteins and their relationship to emulsifying properties
    • Lichan, E.; Nakai, S.; Wood, D. F. Hydrophobicity and solubility of meat proteins and their relationship to emulsifying properties. J. Food Sci. 1984, 49 (2), 345-350.
    • (1984) J. Food Sci , vol.49 , Issue.2 , pp. 345-350
    • Lichan, E.1    Nakai, S.2    Wood, D.F.3
  • 28
    • 84986736089 scopus 로고
    • Relationship between functional (fat binding, emulsifying) and physicochemical properties of muscle proteins - Effects of heating, freezing, pH and species
    • Lichan, E.; Nakai, S.; Wood, D. F. Relationship between functional (fat binding, emulsifying) and physicochemical properties of muscle proteins - Effects of heating, freezing, pH and species. J Food Sci. 1985, 50 (4), 1034-1040.
    • (1985) J Food Sci , vol.50 , Issue.4 , pp. 1034-1040
    • Lichan, E.1    Nakai, S.2    Wood, D.F.3
  • 29
    • 0007511180 scopus 로고
    • The dynamics of thermal-denaturation of fish myosins
    • Chan, J. K.; Gill, T. A.; Paulson, A. T. The dynamics of thermal-denaturation of fish myosins. Food Res. Int. 1992, 25 (2), 117-123.
    • (1992) Food Res. Int , vol.25 , Issue.2 , pp. 117-123
    • Chan, J.K.1    Gill, T.A.2    Paulson, A.T.3
  • 30
    • 0001353395 scopus 로고
    • A heat denaturation study of the 11S globulin in soybean seeds
    • Koshiyama, I.; Hamano, M.; Fukushima, D. A heat denaturation study of the 11S globulin in soybean seeds. Food Chem. 1981, 6 (4), 309-322.
    • (1981) Food Chem , vol.6 , Issue.4 , pp. 309-322
    • Koshiyama, I.1    Hamano, M.2    Fukushima, D.3
  • 31
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Anfinsen, C, Edsall, J, Richards, F, Eisenberg, D, Eds, Academic Press Inc, San Diego, CA
    • Ptitsyn, O. B. Molten globule and protein folding. In Advances in Protein Chemistry; Anfinsen, C., Edsall, J., Richards, F., Eisenberg, D., Eds.; Academic Press Inc.: San Diego, CA, 1995; Vol. 47, pp 83-229.
    • (1995) Advances in Protein Chemistry , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 32
    • 0023658390 scopus 로고
    • Characterization of Cdna coding for the complete light-meromyosin portion of a rabbit fast skeletal-muscle myosin heavy-chain
    • Maeda, K.; Sczakiel, G.; Wittinghofer, A. Characterization of Cdna coding for the complete light-meromyosin portion of a rabbit fast skeletal-muscle myosin heavy-chain. Eur. J. Biochem. 1987, 167 (1), 97-102.
    • (1987) Eur. J. Biochem , vol.167 , Issue.1 , pp. 97-102
    • Maeda, K.1    Sczakiel, G.2    Wittinghofer, A.3
  • 33
    • 0024605313 scopus 로고
    • Thermal unfolding of myosin rod and light-meromyosin - Circular-dichroism and tryptophan fluorescence studies
    • King, L.; Lehrer, S. S. Thermal unfolding of myosin rod and light-meromyosin - Circular-dichroism and tryptophan fluorescence studies. Biochemistry 1989, 28 (8), 3498-3502.
    • (1989) Biochemistry , vol.28 , Issue.8 , pp. 3498-3502
    • King, L.1    Lehrer, S.S.2
  • 34
    • 0001475995 scopus 로고    scopus 로고
    • Lipid oxidation and myosin denaturation in dark chicken meat
    • Li, S. J.; King, A. J. Lipid oxidation and myosin denaturation in dark chicken meat. J. Agric Food. Chem. 1996, 44 (10), 3080-3084.
    • (1996) J. Agric Food. Chem , vol.44 , Issue.10 , pp. 3080-3084
    • Li, S.J.1    King, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.