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Volumn 73, Issue 3, 2008, Pages

Biochemical and conformational changes of myosin purified from Pacific sardine at various pHs

Author keywords

Myosin; Pacific sardine; pH; Solubility

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); FISH PROTEIN; MYOSIN; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN;

EID: 41749111144     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1750-3841.2008.00691.x     Document Type: Article
Times cited : (21)

References (52)
  • 1
    • 10944220493 scopus 로고    scopus 로고
    • Chemical characteristics and lipid fraction quality of sardines (Sardina pilchardus W.): Influence of sex and length
    • Caponio F, Summo C, Bilancia MT, Lestingi A, Laudadio V. 2004. Chemical characteristics and lipid fraction quality of sardines (Sardina pilchardus W.): influence of sex and length. J Appl Ichthyol 20 : 530 5.
    • (2004) J Appl Ichthyol , vol.20 , pp. 530-5
    • Caponio, F.1    Summo, C.2    Bilancia, M.T.3    Lestingi, A.4    Laudadio, V.5
  • 2
    • 0030766542 scopus 로고    scopus 로고
    • Changes in chemical composition and nutritional quality of fried sardine (Clupea pilchardus) produced by frozen storage and microwave reheating
    • Castrillon AM, Navarro P, Alvarez-Pontes E. 1997. Changes in chemical composition and nutritional quality of fried sardine (Clupea pilchardus) produced by frozen storage and microwave reheating. J Sci Food Agric 75 : 125 32.
    • (1997) J Sci Food Agric , vol.75 , pp. 125-32
    • Castrillon, A.M.1    Navarro, P.2    Alvarez-Pontes, E.3
  • 3
    • 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. 1248-53
    • Chan, J.K.1    Gill, T.A.2    Thompson, J.W.3    Singer, D.S.4
  • 6
    • 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. 70-7
    • Ellman, G.L.1
  • 7
    • 0014690519 scopus 로고
    • Subunit structure of myosin III. a proposed model for rabbit skeletal myosin
    • Gershman LC, Stracher A. 1969. Subunit structure of myosin III. A proposed model for rabbit skeletal myosin. J Biol Chem 244 : 2726 36.
    • (1969) J Biol Chem , vol.244 , pp. 2726-36
    • Gershman, L.C.1    Stracher, A.2
  • 8
    • 0002097180 scopus 로고    scopus 로고
    • Physical, chemical and sensory analyses of freshly harvested sardines (Sardina pichardus) stored at 4°C
    • Gokodlu N, Ozden O, Erkan N. 1998. Physical, chemical and sensory analyses of freshly harvested sardines (Sardina pichardus) stored at 4°C. J Aquatic Food Prod Technol 7 : 5 15.
    • (1998) J Aquatic Food Prod Technol , vol.7 , pp. 5-15
    • Gokodlu, N.1    Ozden, O.2    Erkan, N.3
  • 10
    • 84985200365 scopus 로고
    • Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins
    • Hayakawa S, Nakai S. 1985. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. J Food Sci 50 : 486 91.
    • (1985) J Food Sci , vol.50 , pp. 486-91
    • Hayakawa, S.1    Nakai, S.2
  • 11
    • 0018163373 scopus 로고
    • Sulfhydryl and disulfide groups in meats
    • Hofmann K, Hamm R. 1978. Sulfhydryl and disulfide groups in meats. Adv Food Res 24 : 1 111.
    • (1978) Adv Food Res , vol.24 , pp. 1-111
    • Hofmann, K.1    Hamm, R.2
  • 13
    • 0037783116 scopus 로고    scopus 로고
    • Myofibrillar proteins in white muscle of the developing African catfish Heterobranchus longifilis (siluriforms, Clariidae)
    • Huriaux F, Vandewalle P, Baras E, Legendre M, Focant B. 1999. Myofibrillar proteins in white muscle of the developing African catfish Heterobranchus longifilis (siluriforms, Clariidae). Fish Physiol Biochem 21 : 287 301.
    • (1999) Fish Physiol Biochem , vol.21 , pp. 287-301
    • Huriaux, F.1    Vandewalle, P.2    Baras, E.3    Legendre, M.4    Focant, B.5
  • 14
    • 0038189871 scopus 로고    scopus 로고
    • Cryoprotection affects physiochemical attributes of rainbow trout fillets
    • Jittinandana S, Kenney PB, Slider SD. 2003. Cryoprotection affects physiochemical attributes of rainbow trout fillets. Food Chem Toxicol 68 : 1208 14.
    • (2003) Food Chem Toxicol , vol.68 , pp. 1208-14
    • Jittinandana, S.1    Kenney, P.B.2    Slider, S.D.3
  • 15
    • 0021959791 scopus 로고
    • Biochemical characteristics of cardiac myosin: The pH dependence of Ca-ATPase activity, and that of the absorption spectrum of 2,4,6-trinitrophenyl groups attached to myosin
    • Kameyama S, Ichikawa H, Sunaga Y, Nakata S, Saito Y, Eiki T, Watanabe S. 1985. Biochemical characteristics of cardiac myosin: the pH dependence of Ca-ATPase activity, and that of the absorption spectrum of 2,4,6-trinitrophenyl groups attached to myosin. J Biochem 97 : 625 32.
    • (1985) J Biochem , vol.97 , pp. 625-32
    • Kameyama, S.1    Ichikawa, H.2    Sunaga, Y.3    Nakata, S.4    Saito, Y.5    Eiki, T.6    Watanabe, S.7
  • 16
    • 0013947452 scopus 로고
    • Myosin filamentogenesis: Effects of pH and ionic concentration
    • Kaminer B, Bell AL. 1966. Myosin filamentogenesis: effects of pH and ionic concentration. J Mol Biol 20 : 391 401.
    • (1966) J Mol Biol , vol.20 , pp. 391-401
    • Kaminer, B.1    Bell, A.L.2
  • 17
    • 0019331914 scopus 로고
    • Hydrophobicity determined by fluorescence prove method and its correlation with surface properties of proteins
    • Kato A, Nakai S. 1980. Hydrophobicity determined by fluorescence prove method and its correlation with surface properties of proteins. Biochem Biophys Acta 624 : 13 20.
    • (1980) Biochem Biophys Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 19
    • 85008049284 scopus 로고
    • A new method for evaluation of the quality of frozen surimi from Alaska pollack. Relationship between myofibrillar ATPase activity and Kamaboko forming ability of frozen surimi
    • Katoh N, Nozaki H, Komatsu K, Arai K. 1979. A new method for evaluation of the quality of frozen surimi from Alaska pollack. Relationship between myofibrillar ATPase activity and Kamaboko forming ability of frozen surimi. Bull Jpn Soc Sci Fish 45 : 1027 32.
    • (1979) Bull Jpn Soc Sci Fish , vol.45 , pp. 1027-32
    • Katoh, N.1    Nozaki, H.2    Komatsu, K.3    Arai, K.4
  • 20
    • 0347694884 scopus 로고    scopus 로고
    • New approaches for the effective recovery of fish proteins and their physicochemical characteristics
    • Kim YS, Park JW, Choi YJ. 2003. New approaches for the effective recovery of fish proteins and their physicochemical characteristics. Fish Sci 69 : 1231 9.
    • (2003) Fish Sci , vol.69 , pp. 1231-9
    • Kim, Y.S.1    Park, J.W.2    Choi, Y.J.3
  • 21
    • 0021663774 scopus 로고
    • Milk proteins: Physiochemical and functional properties
    • Kinsella JE. 1984. Milk proteins: physiochemical and functional properties. CRC Crit Rev Food Sci Nutr 21 : 197 262.
    • (1984) CRC Crit Rev Food Sci Nutr , vol.21 , pp. 197-262
    • Kinsella, J.E.1
  • 23
    • 0242607667 scopus 로고    scopus 로고
    • Changes in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding
    • Kristinsson HG, Hultin HO. 2003a. Changes in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding. J Agric Food Chem 51 : 7178 96.
    • (2003) J Agric Food Chem , vol.51 , pp. 7178-96
    • Kristinsson, H.G.1    Hultin, H.O.2
  • 24
    • 0042061104 scopus 로고    scopus 로고
    • Effect of low and high pH treatment on the functional properties of cod muscle proteins
    • Kristinsson HG, Hultin HO. 2003b. Effect of low and high pH treatment on the functional properties of cod muscle proteins. J Agric Food Chem 51 : 5103 10.
    • (2003) J Agric Food Chem , vol.51 , pp. 5103-10
    • Kristinsson, H.G.1    Hultin, H.O.2
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 : 680 5.
    • (1970) Nature , vol.227 , pp. 680-5
    • Laemmli, U.K.1
  • 26
    • 33748339636 scopus 로고    scopus 로고
    • Surimi gelation chemistry
    • In: Park, J.W., editor. Boca Raton, Fla.: Taylor & Francis. p
    • Lanier TC, Carvajal P, Yongsawatdigul J. 2005. Surimi gelation chemistry. In : Park JW, editor. Surimi and surimi seafood. Boca Raton, Fla. : Taylor & Francis. p 435 89.
    • (2005) Surimi and Surimi Seafood. , pp. 435-89
    • Lanier, T.C.1    Carvajal, P.2    Yongsawatdigul, J.3
  • 27
    • 0031901189 scopus 로고    scopus 로고
    • Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH
    • Lin TM, Park JW. 1998. Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH. J Food Sci 63 : 215 8.
    • (1998) J Food Sci , vol.63 , pp. 215-8
    • Lin, T.M.1    Park, J.W.2
  • 28
    • 84985287189 scopus 로고
    • Thermal transitions of myosins/subfragments from black marlin (Makaira mazara) ordinary and dark muscles.
    • Lo JR, Mochizuki Y, Nagashima Y, Tanaka M, Iso N, Taguchi T. 1991. Thermal transitions of myosins/subfragments from black marlin (Makaira mazara) ordinary and dark muscles. J Food Sci 56 : 954 7.
    • (1991) J Food Sci , vol.56 , pp. 954-7
    • Lo, J.R.1    Mochizuki, Y.2    Nagashima, Y.3    Tanaka, M.4    Iso, N.5    Taguchi, T.6
  • 29
    • 0034086651 scopus 로고    scopus 로고
    • Gelation characteristics of paddlefish (Polyodon spathula) surimi under different heating conditions
    • Lou X, Wang C, Xiong YL, Wang B, Mims SD. 2000. Gelation characteristics of paddlefish (Polyodon spathula) surimi under different heating conditions. J Food Sci 65 (3 394 8.
    • (2000) J Food Sci , vol.65 , Issue.3 , pp. 394-8
    • Lou, X.1    Wang, C.2    Xiong, Y.L.3    Wang, B.4    Mims, S.D.5
  • 31
    • 84985233021 scopus 로고
    • Actomyosin stabilization to freeze-thaw and heat denaturation by lactate salts
    • MacDonald GA, Lanier TC. 1994. Actomyosin stabilization to freeze-thaw and heat denaturation by lactate salts. J Food Sci 59 : 101 5.
    • (1994) J Food Sci , vol.59 , pp. 101-5
    • MacDonald, G.A.1    Lanier, T.C.2
  • 32
    • 0343487702 scopus 로고    scopus 로고
    • Influence of frozen storage on textural properties of sardine (Sardina pilchardus) mince gels.
    • Marti de Castro MA, Gomez-Guillen MC, Montero P. 1997. Influence of frozen storage on textural properties of sardine (Sardina pilchardus) mince gels. Food Chem 60 : 85 93.
    • (1997) Food Chem , vol.60 , pp. 85-93
    • Marti De Castro, M.A.1    Gomez-Guillen, M.C.2    Montero, P.3
  • 34
    • 33745243695 scopus 로고    scopus 로고
    • Effect of calcium salts on the properties of proteins from oil sardine (Sardinella longiceps) during frozen storage
    • Mathew S, Prakash V. 2006. Effect of calcium salts on the properties of proteins from oil sardine (Sardinella longiceps) during frozen storage. J Food Sci 71 : 178 83.
    • (2006) J Food Sci , vol.71 , pp. 178-83
    • Mathew, S.1    Prakash, V.2
  • 36
    • 0002915720 scopus 로고
    • Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins
    • Monahan FJ, German JB, Kinsella JE. 1995. Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins. J Agric Food Chem 43 : 46 52.
    • (1995) J Agric Food Chem , vol.43 , pp. 46-52
    • Monahan, F.J.1    German, J.B.2    Kinsella, J.E.3
  • 37
    • 84975862233 scopus 로고
    • Physical, chemical and sensory analysis of sardine (Sardina pilchardus) stored in ice
    • Nunes ML, Batista I, De Campos RM. 1992. Physical, chemical and sensory analysis of sardine (Sardina pilchardus) stored in ice. J Sci Food Agric 59 : 37 43.
    • (1992) J Sci Food Agric , vol.59 , pp. 37-43
    • Nunes, M.L.1    Batista, I.2    De Campos, R.M.3
  • 38
    • 26644473633 scopus 로고    scopus 로고
    • Biochemical properties of ordinary and dark muscle myosin from carp skeletal muscle
    • Okagaki T, Takami M, Hosokawa K, Yano M, Fujime SH, Ooi A. 2005. Biochemical properties of ordinary and dark muscle myosin from carp skeletal muscle. J Biochem 138 : 255 62.
    • (2005) J Biochem , vol.138 , pp. 255-62
    • Okagaki, T.1    Takami, M.2    Hosokawa, K.3    Yano, M.4    Fujime, S.H.5    Ooi, A.6
  • 39
    • 0028827160 scopus 로고
    • The effect of pH on the folding and stability of the myosin rod
    • Ozog A, Bechet J. 1995. The effect of pH on the folding and stability of the myosin rod. Eur J Biochem 234 : 501 5.
    • (1995) Eur J Biochem , vol.234 , pp. 501-5
    • Ozog, A.1    Bechet, J.2
  • 40
    • 34248232530 scopus 로고    scopus 로고
    • Extraction of sardine myoglobin and its effect on gelation properties of Pacific whiting surimi
    • Park JD, Park JW. 2007. Extraction of sardine myoglobin and its effect on gelation properties of Pacific whiting surimi. J Food Sci 72 : 202 7.
    • (2007) J Food Sci , vol.72 , pp. 202-7
    • Park, J.D.1    Park, J.W.2
  • 41
    • 36349018024 scopus 로고    scopus 로고
    • Surimi: Manufacturing and evaluation
    • In: Park, J.W. Boca Raton, Fla.: Taylor & Francis. p
    • Park JW, Lin TM. 2005. Surimi: manufacturing and evaluation. In : Park JW. Surimi and surimi seafood. Boca Raton, Fla. : Taylor & Francis. p 33 106.
    • (2005) Surimi and Surimi Seafood. , pp. 33-106
    • Park, J.W.1    Lin, T.M.2
  • 42
    • 84971620957 scopus 로고
    • Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation
    • Sano T, Noguchi SF, Tsuchiya T, Matsumoto JJ. 1988. Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation. J Food Sci 53 : 924 8.
    • (1988) J Food Sci , vol.53 , pp. 924-8
    • Sano, T.1    Noguchi, S.F.2    Tsuchiya, T.3    Matsumoto, J.J.4
  • 43
    • 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. Biochem 29 : 2556 64.
    • (1990) Biochem , vol.29 , pp. 2556-64
    • Shriver, J.W.1    Kamath, U.2
  • 45
    • 3042579438 scopus 로고    scopus 로고
    • Role of pH in solubility and conformational changes of Pacific whiting muscle proteins
    • Thawornchinsombut S, Park JW. 2004. Role of pH in solubility and conformational changes of Pacific whiting muscle proteins. J Food Biochem 28 : 135 54.
    • (2004) J Food Biochem , vol.28 , pp. 135-54
    • Thawornchinsombut, S.1    Park, J.W.2
  • 46
    • 33646377204 scopus 로고    scopus 로고
    • Frozen stability of fish protein isolate under various storage conditions
    • Thawornchinsombut S, Park JW. 2006. Frozen stability of fish protein isolate under various storage conditions. J Food Sci 71 : 227 32.
    • (2006) J Food Sci , vol.71 , pp. 227-32
    • Thawornchinsombut, S.1    Park, J.W.2
  • 47
    • 0037077363 scopus 로고    scopus 로고
    • Differential scanning calorimetry and circular dichroism spectrometry of walleye pollock myosin and light meromyosin
    • Togashi M, Kakinuma M, Nakaya M, Ooi T, Watabe S. 2002. Differential scanning calorimetry and circular dichroism spectrometry of walleye pollock myosin and light meromyosin. J Agric Food Chem 50 : 4803 11.
    • (2002) J Agric Food Chem , vol.50 , pp. 4803-11
    • Togashi, M.1    Kakinuma, M.2    Nakaya, M.3    Ooi, T.4    Watabe, S.5
  • 48
    • 84987339598 scopus 로고
    • Emulsifying property of whey peptide fractions as a function of pH and ionic strength
    • 34
    • Turgeon SL, Gauthier SF, Paquin P. 1992. Emulsifying property of whey peptide fractions as a function of pH and ionic strength. J Food Sci 57 : 601 4, 34.
    • (1992) J Food Sci , vol.57 , pp. 601-4
    • Turgeon, S.L.1    Gauthier, S.F.2    Paquin, P.3
  • 49
    • 0019016536 scopus 로고
    • Myosins from white and dark muscles of mackerel
    • Watabe S, Hashimoto K. 1980. Myosins from white and dark muscles of mackerel. J Biochem 87 : 1491 9.
    • (1980) J Biochem , vol.87 , pp. 1491-9
    • Watabe, S.1    Hashimoto, K.2
  • 50
    • 0040802157 scopus 로고
    • Study of protein solubility during the washing to mechanically deboned chicken meat
    • Yang TS, Froning GW. 1990. Study of protein solubility during the washing to mechanically deboned chicken meat. Poult Sci 69 : 147.
    • (1990) Poult Sci , vol.69 , pp. 147
    • Yang, T.S.1    Froning, G.W.2
  • 51
    • 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 : 679 83.
    • (1999) J Food Sci , vol.64 , pp. 679-83
    • Yongsawatdigul, J.1    Park, J.W.2
  • 52
    • 4744341461 scopus 로고    scopus 로고
    • Effects of alkaline and acid solubilization on gelation characteristics of rockfish muscle proteins
    • Yongsawatdigul J, Park JW. 2004. Effects of alkaline and acid solubilization on gelation characteristics of rockfish muscle proteins. J Food Sci 69 : 499 505.
    • (2004) J Food Sci , vol.69 , pp. 499-505
    • Yongsawatdigul, J.1    Park, J.W.2


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