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Volumn 68, Issue 5, 2003, Pages 1573-1577

Thermal effects on fast skeletal myosins from Alaska pollock, white croaker, and rabbit in relation to gel formation

Author keywords

DSC; Gel formation; Loss modulus; Myosin; Storage modulus

Indexed keywords

GENYONEMUS LINEATUS; ORYCTOLAGUS CUNICULUS; POLLACHIUS VIRENS; THERAGRA CHALCOGRAMMA;

EID: 0038573664     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2003.tb12293.x     Document Type: Article
Times cited : (31)

References (26)
  • 2
    • 0035665007 scopus 로고    scopus 로고
    • Differences in gelation characteristics of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus, and Pricanthus macracanthus
    • Benjakul S, Visessanguan W, Ishizaki S, Tanaka M. 2001. Differences in gelation characteristics of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus, and Pricanthus macracanthus. J Food Sci 66(9):1311-8.
    • (2001) J Food Sci , vol.66 , Issue.9 , pp. 1311-1318
    • Benjakul, S.1    Visessanguan, W.2    Ishizaki, S.3    Tanaka, M.4
  • 3
    • 0031692830 scopus 로고    scopus 로고
    • A conserved C-terminal assembly region in paramyosin and myosin rods
    • Cohen C, Parry DAD. 1998. A conserved C-terminal assembly region in paramyosin and myosin rods. J Struct Biol 122:180-7.
    • (1998) J Struct Biol , vol.122 , pp. 180-187
    • Cohen, C.1    Parry, D.A.D.2
  • 4
    • 21844508379 scopus 로고
    • Rheological parameters as predictor of protein functionary: A model study using myofibrils of different fiber-type composition
    • Egelandsdal B, Martinsen B, Autio K. 1995. Rheological parameters as predictor of protein functionary: a model study using myofibrils of different fiber-type composition. Meat Sci 39:97-111.
    • (1995) Meat Sci , vol.39 , pp. 97-111
    • Egelandsdal, B.1    Martinsen, B.2    Autio, K.3
  • 5
    • 0034838531 scopus 로고    scopus 로고
    • Effect of pH on the rheological and structural properties of gels of water-washed chicken-breast muscle at physiological ionic strength
    • Feng Y, Hultin HO. 2001. Effect of pH on the rheological and structural properties of gels of water-washed chicken-breast muscle at physiological ionic strength. J Agric Food Chem 49(8):3927-35.
    • (2001) J Agric Food Chem , vol.49 , Issue.8 , pp. 3927-3935
    • Feng, Y.1    Hultin, H.O.2
  • 6
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of biuret reaction
    • Gornall AG, Bardawill CJ, David MM. 1949. Determination of serum proteins by means of biuret reaction. J Biol Chem 177:751-65.
    • (1949) J Biol Chem , vol.177 , pp. 751-765
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 8
    • 0025113856 scopus 로고
    • Changes of carp myosin subfragment-1 induced by temperature acclimation
    • Hwang GC, Watabe S, Hashimoto K. 1990. Changes of carp myosin subfragment-1 induced by temperature acclimation. J Comp Physiol B 160(1):141-6.
    • (1990) J Comp Physiol B , vol.160 , Issue.1 , pp. 141-146
    • Hwang, G.C.1    Watabe, S.2    Hashimoto, K.3
  • 9
    • 0005184257 scopus 로고
    • Kamaboko formation of mackerel and red sea bream myosins
    • Iwata K, Kanna K, Okada M. 1977. Kamaboko formation of mackerel and red sea bream myosins. Nippon Suisan Gakkaishi 43(2):237.
    • (1977) Nippon Suisan Gakkaishi , vol.43 , Issue.2 , pp. 237
    • Iwata, K.1    Kanna, K.2    Okada, M.3
  • 10
    • 0032485915 scopus 로고    scopus 로고
    • Thermal unfolding of three acclimation temperature-associated isoforms of carp light meromyosin expressed by recombinant DNAs
    • Kakinuma M, Nakaya M, Hatanaka A, Hirayama Y, Watabe S, Maeda K, Ooi T, Suzuki S. 1998. Thermal unfolding of three acclimation temperature-associated isoforms of carp light meromyosin expressed by recombinant DNAs. Biochemistry 37(18):6606-13.
    • (1998) Biochemistry , vol.37 , Issue.18 , pp. 6606-6613
    • Kakinuma, M.1    Nakaya, M.2    Hatanaka, A.3    Hirayama, Y.4    Watabe, S.5    Maeda, K.6    Ooi, T.7    Suzuki, S.8
  • 11
    • 0033930401 scopus 로고    scopus 로고
    • Differential scanning calorimetry of light meromyosin fragments having various lengths of carp fast skeletal muscle isoforms
    • Kakinuma M, Hatanaka A, Fukushima H, Nakaya M, Maeda K, Doi Y, Ooi T, Watabe S. 2000. Differential scanning calorimetry of light meromyosin fragments having various lengths of carp fast skeletal muscle isoforms. J Biochem 128(1):11-20.
    • (2000) J Biochem , vol.128 , Issue.1 , pp. 11-20
    • Kakinuma, M.1    Hatanaka, A.2    Fukushima, H.3    Nakaya, M.4    Maeda, K.5    Doi, Y.6    Ooi, T.7    Watabe, S.8
  • 12
    • 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. 680-685
    • Laemmli, U.K.1
  • 13
    • 84986736089 scopus 로고
    • Relationship between functional and physicochemical properties of muscle proteins
    • Li-Chan E, Nakai S, Wood D. 1985. Relationship between functional and physicochemical properties of muscle proteins. J Food Sci 50(3):1034-40.
    • (1985) J Food Sci , vol.50 , Issue.3 , pp. 1034-1040
    • Li-Chan, E.1    Nakai, S.2    Wood, D.3
  • 14
    • 0014693726 scopus 로고
    • Substructure of myosin molecule: I. Subfragments of myosin by enzymic degradation
    • Lowry S, Slayter HS, Weeds AG, Baker H. 1969. Substructure of myosin molecule: I. Subfragments of myosin by enzymic degradation. J Cell Biol 42:1-29.
    • (1969) J Cell Biol , vol.42 , pp. 1-29
    • Lowry, S.1    Slayter, H.S.2    Weeds, A.G.3    Baker, H.4
  • 15
    • 0028913571 scopus 로고
    • Differences in the thermal stability of acclimation temperature-associated types of carp myosin and its rod on differential scanning calorimetry
    • Nakaya M, Watabe S, Ooi T. 1995. Differences in the thermal stability of acclimation temperature-associated types of carp myosin and its rod on differential scanning calorimetry. Biochemisty 34(9):3114-20.
    • (1995) Biochemisty , vol.34 , Issue.9 , pp. 3114-3120
    • Nakaya, M.1    Watabe, S.2    Ooi, T.3
  • 16
    • 77956984659 scopus 로고
    • Myosin adenosinetriphospatase
    • Perry SV. 1955. Myosin adenosinetriphospatase. Meth Enzymol 2:582-8.
    • (1955) Meth Enzymol , vol.2 , pp. 582-588
    • Perry, S.V.1
  • 17
    • 84987301296 scopus 로고
    • Action of crude papain on actin and myosin heavy chains isolated from chicken breast muscle
    • Rattrie NW, Regenstein JM. 1977. Action of crude papain on actin and myosin heavy chains isolated from chicken breast muscle. J Food Sci 42(5):1159-63.
    • (1977) J Food Sci , vol.42 , Issue.5 , pp. 1159-1163
    • Rattrie, N.W.1    Regenstein, J.M.2
  • 19
    • 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(3):1412-8.
    • (1981) J Food Sci , vol.46 , Issue.3 , pp. 1412-1418
    • Samejima, K.1    Ishioroshi, M.2    Yasui, T.3
  • 20
    • 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(3):924-8.
    • (1988) J Food Sci , vol.53 , Issue.3 , pp. 924-928
    • Sano, T.1    Noguchi, S.F.2    Tsuchiya, T.3    Matsumoto, J.J.4
  • 21
    • 85008140040 scopus 로고
    • Electron microscopic study of fine structure of kamaboko fish jellies
    • Satoh S, Tsuchiya T, Matsumoto JJ. 1984a. Electron microscopic study of fine structure of kamaboko fish jellies. Nippon Suisan Gakkaishi 50(11):1986-76.
    • (1984) Nippon Suisan Gakkaishi , vol.50 , Issue.11 , pp. 1986-2076
    • Satoh, S.1    Tsuchiya, T.2    Matsumoto, J.J.3
  • 22
    • 85008538342 scopus 로고
    • Electron microscopic study of dispersion profiles of proteins in frozen surimi
    • Satoh S, Tsuchiya T, Matsumoto JJ. 1984b. Electron microscopic study of dispersion profiles of proteins in frozen surimi. Nippon Suisan Gakkaishi 50(12):2117-26.
    • (1984) Nippon Suisan Gakkaishi , vol.50 , Issue.12 , pp. 2117-2126
    • Satoh, S.1    Tsuchiya, T.2    Matsumoto, J.J.3
  • 23
    • 0018609597 scopus 로고
    • Regulatory properties of single-headed fragments of scallop myosin
    • Stafford III WF, Szentkiralyi EM, Szent-Gyorgyi AG. 1979. Regulatory properties of single-headed fragments of scallop myosin. Biochemistry 18(24):5273-80.
    • (1979) Biochemistry , vol.18 , Issue.24 , pp. 5273-5280
    • Stafford W.F. III1    Szentkiralyi, E.M.2    Szent-Gyorgyi, A.G.3
  • 24
    • 0036006643 scopus 로고    scopus 로고
    • Role of neck region in the thermal aggregation of myosin
    • Tazawa T, Kato S, Katoh T, Konno K. 2002. Role of neck region in the thermal aggregation of myosin. J Agric Food Chem 50(1):196-202.
    • (2002) J Agric Food Chem , vol.50 , Issue.1 , pp. 196-202
    • Tazawa, T.1    Kato, S.2    Katoh, T.3    Konno, K.4
  • 25
    • 0037077363 scopus 로고    scopus 로고
    • Differential scanning calorimetry and circular dichroism spectrometry of walleye pollack myosin and light meromyosin
    • Togashi M, Kakimuma M, Nakaya M, Ooi T, Watabe S. 2002. Differential scanning calorimetry and circular dichroism spectrometry of walleye pollack myosin and light meromyosin. J Agric Food Chem 50(17):4756-802.
    • (2002) J Agric Food Chem , vol.50 , Issue.17 , pp. 4756-4802
    • Togashi, M.1    Kakimuma, M.2    Nakaya, M.3    Ooi, T.4    Watabe, S.5
  • 26
    • 0034055958 scopus 로고    scopus 로고
    • Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin
    • Visessanguan W, Ogawa M, Nakai S, An H. 2000. Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin. J Agric Food Chem 48(4):1016-23.
    • (2000) J Agric Food Chem , vol.48 , Issue.4 , pp. 1016-1023
    • Visessanguan, W.1    Ogawa, M.2    Nakai, S.3    An, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.