메뉴 건너뛰기




Volumn 72, Issue 3, 1996, Pages 367-375

Determination of surface hydrophobicity of fast and slow myosins from rabbit skeletal muscles: Implication in heat-induced gelation

Author keywords

heat induced gelation; heating; muscle type; myosin; surface hydrophobicity

Indexed keywords


EID: 0029999544     PISSN: 00225142     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0010(199611)72:3<367::AID-JSFA668>3.0.CO;2-D     Document Type: Article
Times cited : (42)

References (44)
  • 1
    • 0021782026 scopus 로고
    • Functionality of muscle proteins in gelation mechanisms of structured meat products
    • Asghar A 1985 Functionality of muscle proteins in gelation mechanisms of structured meat products. CRC Crit Rev Food Sci 1 27-106.
    • (1985) CRC Crit Rev Food Sci , vol.1 , pp. 27-106
    • Asghar, A.1
  • 2
    • 0021131036 scopus 로고
    • Biochemical and functional characteristics of myosin from red and white muscles of chicken as influenced by nutritional stress
    • Asghar A, Monta J, Samejima K, Yasui T 1984 Biochemical and functional characteristics of myosin from red and white muscles of chicken as influenced by nutritional stress. Agric Biol Chem 48 2217-2224.
    • (1984) Agric Biol Chem , vol.48 , pp. 2217-2224
    • Asghar, A.1    Monta, J.2    Samejima, K.3    Yasui, T.4
  • 3
    • 0014117822 scopus 로고
    • On the average hydrophobicity of proteins and the relation between it and protein structure
    • Bigelow C C 1967 On the average hydrophobicity of proteins and the relation between it and protein structure. J Theoret Biol 16 187-211.
    • (1967) J Theoret Biol , vol.16 , pp. 187-211
    • Bigelow, C.C.1
  • 4
    • 0020537655 scopus 로고
    • Mapping of hydrophobic sites on the surface of myosin and its fragments
    • Borejdo J 1983 Mapping of hydrophobic sites on the surface of myosin and its fragments. Biochemistry 22 1182-1187.
    • (1983) Biochemistry , vol.22 , pp. 1182-1187
    • Borejdo, J.1
  • 5
    • 10544222790 scopus 로고
    • Heat-gelation of myosin: Influence of purification, muscle type and ionic strength
    • Clermont-Fd, France
    • Boyer C, Ouali A, Culioli J 1992 Heat-gelation of myosin: Influence of purification, muscle type and ionic strength. In: 38th Int Cong Meat Sci Technol (Vol 5). Clermont-Fd, France, pp 1023-1026.
    • (1992) 38th Int Cong Meat Sci Technol , vol.5 , pp. 1023-1026
    • Boyer, C.1    Ouali, A.2    Culioli, J.3
  • 6
    • 84985181134 scopus 로고
    • Heat-induced gelation of myosins/subfragments from chicken leg and breast muscles at high ionic strength and low pH
    • Choe I S, Monta J I, Yamamoto K, Samejima K, Yasui T 1991 Heat-induced gelation of myosins/subfragments from chicken leg and breast muscles at high ionic strength and low pH. J Food Sci 56 884-890.
    • (1991) J Food Sci , vol.56 , pp. 884-890
    • Choe, I.S.1    Monta, J.I.2    Yamamoto, K.3    Samejima, K.4    Yasui, T.5
  • 7
    • 21144466646 scopus 로고
    • Heat-induced gelation properties of myosin: Influence of purification and muscle type
    • Culioli J, Boyer C, Vignon X, Ouali A 1993 Heat-induced gelation properties of myosin: Influence of purification and muscle type. Sci Aliments 13 249-260.
    • (1993) Sci Aliments , vol.13 , pp. 249-260
    • Culioli, J.1    Boyer, C.2    Vignon, X.3    Ouali, A.4
  • 8
    • 0024321591 scopus 로고
    • Lysosomal proteinase-sensitive regions in fast and slow skeletal muscle myosin
    • Dufour E, Ouali A, Obled A, Deval C, Valin C 1989 Lysosomal proteinase-sensitive regions in fast and slow skeletal muscle myosin. Biochimie 71 625-632.
    • (1989) Biochimie , vol.71 , pp. 625-632
    • Dufour, E.1    Ouali, A.2    Obled, A.3    Deval, C.4    Valin, C.5
  • 9
    • 84985398393 scopus 로고
    • Dynamic rheological measurements on heat-induced myosin gels: Effect of ionic strength, protein concentration and addition of adenosine triphosphate or pyrophosphate
    • Egelandsdal B, Fretheim K, Samejima K 1986 Dynamic rheological measurements on heat-induced myosin gels: Effect of ionic strength, protein concentration and addition of adenosine triphosphate or pyrophosphate. J Sci Food Agric 37 915-926.
    • (1986) J Sci Food Agric , vol.37 , pp. 915-926
    • Egelandsdal, B.1    Fretheim, K.2    Samejima, K.3
  • 11
    • 85008377080 scopus 로고
    • Functional differences of myofibrillar proteins from fast and slow-twitch muscles
    • Foegeding E A, Liu M N 1995 Functional differences of myofibrillar proteins from fast and slow-twitch muscles. J Muscle Foods 6 109-123.
    • (1995) J Muscle Foods , vol.6 , pp. 109-123
    • Foegeding, E.A.1    Liu, M.N.2
  • 12
    • 3342926442 scopus 로고
    • Recent advances in the study of myosin and myofibril gel formation
    • Albena, Bulgaria
    • Fretheim K, Egelandsdal B, Harbitz B, Samejima K 1985 Recent advances in the study of myosin and myofibril gel formation. In: 31st Eur Cong Meat Res Work (Vol 1). Albena, Bulgaria, pp 219-223.
    • (1985) 31st Eur Cong Meat Res Work , vol.1 , pp. 219-223
    • Fretheim, K.1    Egelandsdal, B.2    Harbitz, B.3    Samejima, K.4
  • 13
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of Biuret reaction
    • Gornall A G, Bardawill C J, David M M 1949 Determination of serum proteins by means of Biuret reaction. J Biol Chem 177 751-766.
    • (1949) J Biol Chem , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 15
    • 0040347772 scopus 로고
    • Aspects of protein structure, rheology and texturisation
    • ed Sherman P. Academic Press, London
    • Hermansson A M 1979 Aspects of protein structure, rheology and texturisation. In: Food Texture and Rheology, ed Sherman P. Academic Press, London, pp 265-282.
    • (1979) Food Texture and Rheology , pp. 265-282
    • Hermansson, A.M.1
  • 17
    • 84985262237 scopus 로고
    • Heat-induced gelation of myosin: Factors of pH and salt concentrations
    • Ishioroshi M, Samejima K, Yasui T 1979 Heat-induced gelation of myosin: Factors of pH and salt concentrations. J Food Sci 44 1280-1284.
    • (1979) J Food Sci , vol.44 , pp. 1280-1284
    • Ishioroshi, M.1    Samejima, K.2    Yasui, T.3
  • 18
    • 84985225735 scopus 로고
    • Further studies on the role of head and tail regions of the myosin molecule in heat-induced gelation
    • Ishioroshi M, Samejima K, Yasui T 1981 Further studies on the role of head and tail regions of the myosin molecule in heat-induced gelation. J Food Sci 47 114-120.
    • (1981) J Food Sci , vol.47 , pp. 114-120
    • Ishioroshi, M.1    Samejima, K.2    Yasui, T.3
  • 19
    • 84985251632 scopus 로고
    • Fish myosin fragments solubility and ANS-fluorescence intensity affected by n-butanol
    • Ishizaki S, Lin W L, Tanaka M, Taguchi T, Amano K 1994 Fish myosin fragments solubility and ANS-fluorescence intensity affected by n-butanol. J Food Sci 59 97-100.
    • (1994) J Food Sci , vol.59 , pp. 97-100
    • Ishizaki, S.1    Lin, W.L.2    Tanaka, M.3    Taguchi, T.4    Amano, K.5
  • 20
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • Kato A, Nakai S 1980 Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim Biophys Acta 624 13-20.
    • (1980) Biochim Biophys Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriophage T4
    • Laemmli J 1970 Cleavage of structural proteins during the assembly of bacteriophage T4. Nature 227 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, J.1
  • 22
    • 0002609034 scopus 로고
    • Relationships of hydrophobicity to emulsifying properties of heat-denatured proteins
    • Leandros P, Voutsinas E C, Nakai S 1983 Relationships of hydrophobicity to emulsifying properties of heat-denatured proteins. J Food Sci 48 26-32.
    • (1983) J Food Sci , vol.48 , pp. 26-32
    • Leandros, P.1    Voutsinas, E.C.2    Nakai, S.3
  • 23
    • 84985266593 scopus 로고
    • Hydrophobicity and solubility of meat proteins and their relationship to emulsifying properties
    • Li Chan E, Nakai S, Wood D F 1984 Hydrophobicity and solubility of meat proteins and their relationship to emulsifying properties. J Food Sci 49 345-350.
    • (1984) J Food Sci , vol.49 , pp. 345-350
    • Li Chan, E.1    Nakai, S.2    Wood, D.F.3
  • 24
    • 84985262153 scopus 로고
    • Muscle protein structure-function relationships and discrimination of functionality by multivariate analysis
    • Li Chan E, Nakai S, Wood D F 1987 Muscle protein structure-function relationships and discrimination of functionality by multivariate analysis. J Food Sci 52 31-41.
    • (1987) J Food Sci , vol.52 , pp. 31-41
    • Li Chan, E.1    Nakai, S.2    Wood, D.F.3
  • 25
    • 0005187404 scopus 로고
    • Involvement of hydrophobic residues in heat-induced gelation of myosin tail subfragments from rabbit skeletal muscle
    • Monta J I, Yasui T 1991 Involvement of hydrophobic residues in heat-induced gelation of myosin tail subfragments from rabbit skeletal muscle. Agric Biol Chem 55 597-599.
    • (1991) Agric Biol Chem , vol.55 , pp. 597-599
    • Monta, J.I.1    Yasui, T.2
  • 26
    • 0027350716 scopus 로고
    • Recent advances in structure and function of food proteins: QSAR approach
    • Nakai S, Li-Chan E 1993 Recent advances in structure and function of food proteins: QSAR approach. CRC Crit Rev Food Sci Nutr 33 477-499.
    • (1993) CRC Crit Rev Food Sci Nutr , vol.33 , pp. 477-499
    • Nakai, S.1    Li-Chan, E.2
  • 27
    • 84982613959 scopus 로고
    • Contribution of protein hydrophobicity to its functionality
    • Nakai S, Li-Chang E, Hayakawa S 1986 Contribution of protein hydrophobicity to its functionality. Die Nahrung 30 327-336.
    • (1986) Die Nahrung , vol.30 , pp. 327-336
    • Nakai, S.1    Li-Chang, E.2    Hayakawa, S.3
  • 28
    • 0015924821 scopus 로고
    • A new protein of the thick filaments of vertebrate skeletal myofibrils
    • Offer G, Moos C, Starr R 1973 A new protein of the thick filaments of vertebrate skeletal myofibrils. J Molec Biol 74 653-676.
    • (1973) J Molec Biol , vol.74 , pp. 653-676
    • Offer, G.1    Moos, C.2    Starr, R.3
  • 29
    • 10544253810 scopus 로고
    • Caractérisation des propriétés hydrophobes de la myosine de différents types musculaires
    • Ouali A, Gatellier P, Dufour E 1988 Caractérisation des propriétés hydrophobes de la myosine de différents types musculaires. Viandes et Prod Carnés 9 198.
    • (1988) Viandes et Prod Carnés , vol.9 , pp. 198
    • Ouali, A.1    Gatellier, P.2    Dufour, E.3
  • 30
    • 0015507609 scopus 로고
    • 1-Anilinonaphtalene-8-sulfonate the dependance of emission spectra on molecular conformation studied by fluorescence and proton-magnetic resonance
    • Penzer G 1972 1-Anilinonaphtalene-8-sulfonate The dependance of emission spectra on molecular conformation studied by fluorescence and proton-magnetic resonance. Eur J Biochem 25 218-228.
    • (1972) Eur J Biochem , vol.25 , pp. 218-228
    • Penzer, G.1
  • 31
    • 0019692787 scopus 로고
    • Protein functionality: Classification, definition and methodology
    • Protein Functionality in Foods, ed Cherry J P. Washington, DC, USA
    • Pour El A 1981 Protein functionality: Classification, definition and methodology. In: Protein Functionality in Foods, (ACS Symp Ser 147, Vol 1) ed Cherry J P. Washington, DC, USA, pp 1-19.
    • (1981) ACS Symp Ser 147 , vol.1 , pp. 1-19
    • Pour El, A.1
  • 32
    • 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 1981 Relative roles of the head and tail portions of the molecule in heat-induced gelation of myosin. J Food Sci 46 1412-1418.
    • (1981) J Food Sci , vol.46 , pp. 1412-1418
    • Samejima, K.1    Ishioroshi, M.2    Yasui, T.3
  • 33
    • 84971620957 scopus 로고
    • Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation
    • Sano T, Noguchi S F, Tsuchiya T, Matsumoto J J 1988 Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation. J Food Sci 53 924-928.
    • (1988) J Food Sci , vol.53 , pp. 924-928
    • Sano, T.1    Noguchi, S.F.2    Tsuchiya, T.3    Matsumoto, J.J.4
  • 35
    • 0002125934 scopus 로고
    • The mechanisms of formation of gels from myosin molecules
    • Sharp A, Offer G 1992 The mechanisms of formation of gels from myosin molecules. J Sci Food Agric 58 63-73.
    • (1992) J Sci Food Agric , vol.58 , pp. 63-73
    • Sharp, A.1    Offer, G.2
  • 36
    • 0012926654 scopus 로고
    • Conjugated polyene fatty acids as membrane probes: Preliminary characterization
    • Sklar L A, Hudson B S, Simoni R D 1975 Conjugated polyene fatty acids as membrane probes: Preliminary characterization. Proc Natl Acad Sci USA 72 1649-1653.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 1649-1653
    • Sklar, L.A.1    Hudson, B.S.2    Simoni, R.D.3
  • 37
    • 0017661379 scopus 로고
    • Conjugated polyene fatty acids as fluorescent probes: Binding to bovine serum albumin
    • Sklar L A, Hudson B S, Simoni R D 1977 Conjugated polyene fatty acids as fluorescent probes: Binding to bovine serum albumin. Biochemistry 16 5100-5108.
    • (1977) Biochemistry , vol.16 , pp. 5100-5108
    • Sklar, L.A.1    Hudson, B.S.2    Simoni, R.D.3
  • 38
    • 0000845340 scopus 로고
    • Meat proteins: Functional properties in communited meat products
    • Smith D M 1988 Meat proteins: Functional properties in communited meat products. Food Technol 42 116-121.
    • (1988) Food Technol , vol.42 , pp. 116-121
    • Smith, D.M.1
  • 40
    • 0002206625 scopus 로고
    • Water activity and its estimation in food systems: Theoretical aspects
    • eds Rockland L B & Stewart G F. Academic Press, New York, USA
    • Van den Berg C, Bruin S 1981 Water activity and its estimation in food systems: Theoretical aspects. In: Water Activity: Influences on Food Quality, eds Rockland L B & Stewart G F. Academic Press, New York, USA, pp 1-61.
    • (1981) Water Activity: Influences on Food Quality , pp. 1-61
    • Van Den Berg, C.1    Bruin, S.2
  • 41
    • 0001679156 scopus 로고
    • The effects of neutral salts on the structure and conformational stability of macromolecules in solution
    • eds Timasheff S N & Fasman G D. Marcel Dekker Inc, New York, USA
    • Von Hippel P H, Schleich T 1969 The effects of neutral salts on the structure and conformational stability of macromolecules in solution. In: Structure and Stability of Biological Macromolecules, eds Timasheff S N & Fasman G D. Marcel Dekker Inc, New York, USA, pp 417-574.
    • (1969) Structure and Stability of Biological Macromolecules , pp. 417-574
    • Von Hippel, P.H.1    Schleich, T.2
  • 42
    • 0014443655 scopus 로고
    • Comparative studies on myosins from breast and leg muscle of chicken
    • Wu C 1969 Comparative studies on myosins from breast and leg muscle of chicken. Biochemistry 8 39-45.
    • (1969) Biochemistry , vol.8 , pp. 39-45
    • Wu, C.1
  • 43
    • 0028311361 scopus 로고
    • Myofibrillar protein from different muscle fiber type: Implications of biochemical and functional properties in meat processing
    • Xiong Y L 1994 Myofibrillar protein from different muscle fiber type: Implications of biochemical and functional properties in meat processing. CRC Crit Rev Food Sci Nutr 34 293-320.
    • (1994) CRC Crit Rev Food Sci Nutr , vol.34 , pp. 293-320
    • Xiong, Y.L.1
  • 44
    • 10544221197 scopus 로고
    • Recent advances in meat science in Japan - Functionality of muscle proteins in gelation mechanism of structured meat products
    • Yasui T, Samejima K 1990 Recent advances in meat science in Japan - Functionality of muscle proteins in gelation mechanism of structured meat products. JARQ 24 131-140.
    • (1990) JARQ , vol.24 , pp. 131-140
    • Yasui, T.1    Samejima, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.