메뉴 건너뛰기




Volumn 51, Issue 24, 2003, Pages 7187-7196

Changes in Conformation and Subunit Assembly of Cod Myosin at Low and High pH and after Subsequent Refolding

Author keywords

Acid pH; Alkaline pH; Cod myosin; Conformational changes; Molten globule; Refolding; Unfolding

Indexed keywords

ACID; ADENOSINE TRIPHOSPHATASE; MYOSIN; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN; PROTEIN SUBUNIT; THIOL DERIVATIVE;

EID: 0242607667     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf026193m     Document Type: Article
Times cited : (208)

References (46)
  • 1
    • 0001954905 scopus 로고    scopus 로고
    • Functional chicken muscle protein isolates prepared using low ionic strength, acid solubilization/precipitation
    • Kelleher, S. D.; Hultin, H. O. Functional chicken muscle protein isolates prepared using low ionic strength, acid solubilization/precipitation. Reciprocal Meat Conf. Prooc. 2000, 53, 76-81.
    • (2000) Reciprocal Meat Conf. Prooc. , vol.53 , pp. 76-81
    • Kelleher, S.D.1    Hultin, H.O.2
  • 2
    • 0012079119 scopus 로고    scopus 로고
    • Functional fish protein isolates prepared using low ionic strength, acid solubilization/precipitation
    • in Print
    • Kelleher S. D.; Feng Y.; Kristinsson H. G.; Hultin H. O.; McClements D. J. 2002. Functional fish protein isolates prepared using low ionic strength, acid solubilization/precipitation. Fisheries Sci., in Print.
    • (2002) Fisheries Sci.
    • Kelleher, S.D.1    Feng, Y.2    Kristinsson, H.G.3    Hultin, H.O.4    McClements, D.J.5
  • 3
    • 77955655072 scopus 로고    scopus 로고
    • Structure-function relationships of muscle proteins
    • S. Damodara and A. Paraf, Eds.; Marcel Dekker: New York
    • Xiong, Y. L. Structure-function relationships of muscle proteins. In Food Proteins and Their Applications; S. Damodara and A. Paraf, Eds.; Marcel Dekker: New York, 1997; pp 341-392.
    • (1997) Food Proteins and Their Applications , pp. 341-392
    • Xiong, Y.L.1
  • 4
    • 0002878025 scopus 로고
    • The structural basis of water-holding in meat. Part 1: General principles and water-uptake in meat processing
    • R. Lawrie, Ed.; Elsevier Applied Science Publishers: London
    • Offer, G.; Knight, P. The structural basis of water-holding in meat. Part 1: General principles and water-uptake in meat processing. In Developments in Meat Science; R. Lawrie, Ed.; Elsevier Applied Science Publishers: London, 1988; pp 63-172.
    • (1988) Developments in Meat Science , pp. 63-172
    • Offer, G.1    Knight, P.2
  • 5
    • 0002312592 scopus 로고    scopus 로고
    • Characteristics of edible muscle tissue
    • O. R. Fennema, Ed.; Marcel Dekker: New York
    • Foegeding, E. A.; Lanier, T. C.; Hultin, H. O. Characteristics of edible muscle tissue. In Food Chemistry; O. R. Fennema, Ed.; Marcel Dekker: New York, 1996; pp 879-942.
    • (1996) Food Chemistry , pp. 879-942
    • Foegeding, E.A.1    Lanier, T.C.2    Hultin, H.O.3
  • 6
    • 0019975166 scopus 로고
    • Periodic charge distribution in the myosin rod amino acid sequence match cross-bridge spacings in muscle
    • McLachlan, A. D.; Kam, J. Periodic charge distribution in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature 1982, 299, 226-234.
    • (1982) Nature , vol.299 , pp. 226-234
    • McLachlan, A.D.1    Kam, J.2
  • 7
    • 0028827160 scopus 로고
    • The effect of pH on the folding and stability of the myosin rod
    • Ozog, A.; Bechet, J.-J. The effect of pH on the folding and stability of the myosin rod. Eur. J. Biochem. 1995, 234, 501-505.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 501-505
    • Ozog, A.1    Bechet, J.-J.2
  • 8
    • 0004161470 scopus 로고    scopus 로고
    • Oxford University Press: Oxford, UK
    • Sellers, J. R. Myosins, 2 ed.; Oxford University Press: Oxford, UK, 1999.
    • (1999) Myosins, 2 Ed.
    • Sellers, J.R.1
  • 9
    • 0015502632 scopus 로고
    • Geometry of the myosin dimer in high-salt media. I. Association behavior of rod segments from myosin
    • Harrington, W. F.; Burke, M. Geometry of the myosin dimer in high-salt media. I. Association behavior of rod segments from myosin. Biochemistry 1972, 11, 1448-1455.
    • (1972) Biochemistry , vol.11 , pp. 1448-1455
    • Harrington, W.F.1    Burke, M.2
  • 11
    • 0025856806 scopus 로고
    • Denatured states of proteins
    • Dill, K. A.; Shortle, D. Denatured states of proteins. Annu. Rev. Biochem. 1991, 60, 795-825.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 795-825
    • Dill, K.A.1    Shortle, D.2
  • 12
    • 0024963570 scopus 로고
    • Conformational states of β-lactamase: Molten-globule states at acidic and alkaline pH with high salt
    • Goto, Y.; Fink, A. L. Conformational states of β-lactamase: Molten-globule states at acidic and alkaline pH with high salt. Biochemistry 1989, 28, 945-952.
    • (1989) Biochemistry , vol.28 , pp. 945-952
    • Goto, Y.1    Fink, A.L.2
  • 14
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins: Intermediates and unfolded states
    • Fink, A. L.; Calciano, L. J.; Goto, Y.; Kurotsu, T.; Palleros, D. R. Classification of acid denaturation of proteins: Intermediates and unfolded states. Biochemistry 1994, 33, 12504-12511.
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.R.5
  • 16
    • 0000820879 scopus 로고
    • Comparative study of the alpha-helical muscle proteins
    • Lowey, S. Comparative study of the alpha-helical muscle proteins. J. Biol. Chem. 1965, 240, 2421-2427.
    • (1965) J. Biol. Chem. , vol.240 , pp. 2421-2427
    • Lowey, S.1
  • 19
    • 0015991899 scopus 로고
    • The dissociation of myosin in acid
    • Szuchet, S.; Zobel, C. R. The dissociation of myosin in acid. Biochemistry 1974, 13, 1482-1491.
    • (1974) Biochemistry , vol.13 , pp. 1482-1491
    • Szuchet, S.1    Zobel, C.R.2
  • 20
    • 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, 249-256.
    • (2001) J. Food Biochem. , vol.25 , pp. 249-256
    • Kristinsson, H.G.1
  • 21
    • 0000252971 scopus 로고
    • On the solubility of cod muscle proteins in water
    • Stefansson, G.; Hultin, H. O. On the solubility of cod muscle proteins in water. J. Agric. Food Chem. 1994, 42, 2656-2664.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 2656-2664
    • Stefansson, G.1    Hultin, H.O.2
  • 25
    • 0031901189 scopus 로고    scopus 로고
    • Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH
    • Lin, T. M.; Park, J. W. Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH. J. Food Sci. 1998, 63, 215-218.
    • (1998) J. Food Sci. , vol.63 , pp. 215-218
    • Lin, T.M.1    Park, J.W.2
  • 26
    • 77956984659 scopus 로고
    • Myosin adenosine triphosphatase
    • Perry, S. V. Myosin adenosine triphosphatase. Methods Enzymol. 1955, 2, 582-589.
    • (1955) Methods Enzymol. , vol.2 , pp. 582-589
    • Perry, S.V.1
  • 27
    • 0011807556 scopus 로고
    • Denaturation of cod myosin during freezing after modification with formaldehyde
    • Ang, J. F.; Hultin, H. O. Denaturation of cod myosin during freezing after modification with formaldehyde. J. Food Sci. 1989, 54, 814-818.
    • (1989) J. Food Sci. , vol.54 , pp. 814-818
    • Ang, J.F.1    Hultin, H.O.2
  • 28
    • 0024605313 scopus 로고
    • Thermal unfolding of myosin rod and light meromyosin: Circular dichrosim and tryptophan fluorescence studies
    • King, L.; Lehrer, S. S. Thermal unfolding of myosin rod and light meromyosin: Circular dichrosim and tryptophan fluorescence studies. Biochemistry 1989, 28, 3498-3502.
    • (1989) Biochemistry , vol.28 , pp. 3498-3502
    • King, L.1    Lehrer, S.S.2
  • 29
    • 0242570234 scopus 로고
    • Effect of pH and urea on the optical rotation, viscosity, and adenosine triphosphatase activity of myosin A
    • Stracher, A. Effect of pH and urea on the optical rotation, viscosity, and adenosine triphosphatase activity of myosin A. J. Biol. Chem. 1961, 236, 2467-2471.
    • (1961) J. Biol. Chem. , vol.236 , pp. 2467-2471
    • Stracher, A.1
  • 30
    • 0023626273 scopus 로고
    • Protein folding: Hypotheses and experiments
    • Ptitsyn, O. B. Protein folding: hypotheses and experiments. J. Protein Chem. 1987, 6, 273-293.
    • (1987) J. Protein Chem. , vol.6 , pp. 273-293
    • Ptitsyn, O.B.1
  • 31
    • 0027543524 scopus 로고
    • Molten globule state of food proteins
    • Hirose, M. Molten globule state of food proteins. Trends Food Sci. Technol. 1993, 4, 48-51.
    • (1993) Trends Food Sci. Technol. , vol.4 , pp. 48-51
    • Hirose, M.1
  • 32
    • 0014944782 scopus 로고
    • Relationship of structure to function in myosin. I. Subunit dissociation in concentrated salt solutions
    • Gershman, L. C.; Dreizen, P. Relationship of structure to function in myosin. I. Subunit dissociation in concentrated salt solutions. Biochemistry 1970, 9, 1677-1687.
    • (1970) Biochemistry , vol.9 , pp. 1677-1687
    • Gershman, L.C.1    Dreizen, P.2
  • 33
    • 0000049742 scopus 로고
    • Contractile proteins of muscle
    • H. Neurath and R. L. Hill, Eds.; Academic Press: New York
    • Harrington, W. F. Contractile proteins of muscle. In The Proteins; H. Neurath and R. L. Hill, Eds.; Academic Press: New York, 1979; pp 245-409.
    • (1979) The Proteins , pp. 245-409
    • Harrington, W.F.1
  • 34
    • 21144484185 scopus 로고
    • Isolation of carp myosin rod and its structural stability
    • Kato, S.; Konno, K. Isolation of carp myosin rod and its structural stability. Nippon Suisan Gakkaishi 1993, 59, 539-544.
    • (1993) Nippon Suisan Gakkaishi , vol.59 , pp. 539-544
    • Kato, S.1    Konno, K.2
  • 35
    • 0027372445 scopus 로고
    • Tryptophan fluorescence quenching in rabbit skeletal myosin rod
    • Chang, Y. C.; Ludescher, R. D. Tryptophan fluorescence quenching in rabbit skeletal myosin rod. Biophys. Chem. 1993, 48, 49-59.
    • (1993) Biophys. Chem. , vol.48 , pp. 49-59
    • Chang, Y.C.1    Ludescher, R.D.2
  • 36
    • 0030943106 scopus 로고    scopus 로고
    • Functional analysis of the chicken sarcomeric myosin rod: Regulation of dimerization, solubility, and fibrillogenesis
    • Bandman, E.; Arrizubieta, M.-J.; Wick, M.; Hattori, A.; Tablin, F.; Zhang, S.; Zhang, Q. Functional analysis of the chicken sarcomeric myosin rod: Regulation of dimerization, solubility, and fibrillogenesis. Cell Struct. Funct. 1997, 22, 131-137.
    • (1997) Cell Struct. Funct. , vol.22 , pp. 131-137
    • Bandman, E.1    Arrizubieta, M.-J.2    Wick, M.3    Hattori, A.4    Tablin, F.5    Zhang, S.6    Zhang, Q.7
  • 37
    • 0003328372 scopus 로고
    • The denaturation of paramyosin and tropomyosin by guanidine hydrochloride
    • J. Gergely, Ed.; Little, Brown, and Co.: Boston, MA
    • Noelken, M.; Holtzer, A. M. The denaturation of paramyosin and tropomyosin by guanidine hydrochloride. In Biochemistry of Muscle Contraction; J. Gergely, Ed.; Little, Brown, and Co.: Boston, MA, 1964; pp 374-378.
    • (1964) Biochemistry of Muscle Contraction , pp. 374-378
    • Noelken, M.1    Holtzer, A.M.2
  • 38
    • 0242570241 scopus 로고
    • Myosin substructure: Isolation of a helical subunit from heavy meromyosin
    • Lowey, S. Myosin substructure: isolation of a helical subunit from heavy meromyosin. Science 1964, 597, 145-147.
    • (1964) Science , vol.597 , pp. 145-147
    • Lowey, S.1
  • 39
    • 0023506457 scopus 로고
    • Folding and association of proteins
    • Jaenicke, R. Folding and association of proteins. Prog. Biophys. Mol. Biol. 1987, 49, 117-237.
    • (1987) Prog. Biophys. Mol. Biol. , vol.49 , pp. 117-237
    • Jaenicke, R.1
  • 40
    • 0033956125 scopus 로고    scopus 로고
    • Conformational issues in the characterization of proteins
    • Price, N. C. Conformational issues in the characterization of proteins. Biotechnol. Appl. Biochem. 2000, 31, 29-40.
    • (2000) Biotechnol. Appl. Biochem. , vol.31 , pp. 29-40
    • Price, N.C.1
  • 41
    • 0033970020 scopus 로고    scopus 로고
    • Folding and binding cascades: Dynamic landscapes and population shifts
    • Kumar, S.; Ma, B.; Tsai, C.-J.; Sinha, N.; Nussinov, R. Folding and binding cascades: Dynamic landscapes and population shifts. Protein Sci. 2000, 9, 10-19.
    • (2000) Protein Sci. , vol.9 , pp. 10-19
    • Kumar, S.1    Ma, B.2    Tsai, C.-J.3    Sinha, N.4    Nussinov, R.5
  • 42
    • 0025732289 scopus 로고
    • Assembly of avian skeletal muscle myosins: Evidence that homodimers of the heavy chain subunit are the thermodynamically stable form
    • Kerwin, B.; Bandman, E. Assembly of avian skeletal muscle myosins: Evidence that homodimers of the heavy chain subunit are the thermodynamically stable form. J. Cell Biol. 1991, 113, 311-320.
    • (1991) J. Cell Biol. , vol.113 , pp. 311-320
    • Kerwin, B.1    Bandman, E.2
  • 43
    • 0027331575 scopus 로고
    • Unfolding/refolding studies of the myosin rod
    • Nozais, A.; Bechet, J.-J. Unfolding/refolding studies of the myosin rod. Eur. J. Biochem. 1993, 218, 1049-1055.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 1049-1055
    • Nozais, A.1    Bechet, J.-J.2
  • 44
    • 0017761088 scopus 로고
    • Fluorescence depolarization studies on the flexibility of the myosin rod
    • Harvey, S. C.; Cheung, H. C. Fluorescence depolarization studies on the flexibility of the myosin rod. Biochemistry 1977, 16, 5181-5187.
    • (1977) Biochemistry , vol.16 , pp. 5181-5187
    • Harvey, S.C.1    Cheung, H.C.2
  • 45
    • 0032429619 scopus 로고    scopus 로고
    • Disulfide bonds influence the heat-induced gel properties of chicken breast muscle myosin
    • Smyth, A. B.; Smith, D. M.; O'Neill, E. Disulfide bonds influence the heat-induced gel properties of chicken breast muscle myosin. J. Food. Sci. 1998, 63, 584-588.
    • (1998) J. Food. Sci. , vol.63 , pp. 584-588
    • Smyth, A.B.1    Smith, D.M.2    O'Neill, E.3
  • 46
    • 0014350667 scopus 로고
    • The substructure of the myosin molecule. Production and properties of the alkali subunits
    • Frederiksen, D. W.; Holtzer, A. The substructure of the myosin molecule. Production and properties of the alkali subunits. Biochemistry 1968, 7, 3935-3940.
    • (1968) Biochemistry , vol.7 , pp. 3935-3940
    • Frederiksen, D.W.1    Holtzer, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.