메뉴 건너뛰기




Volumn 71, Issue 2, 2005, Pages 405-413

Species-specific thermal denaturation pattern of fish myosin when heated as myofibrils as studied by myosin subfragment-1 and rod denaturation rates

Author keywords

F actin; Myofibril; Myosin; Species specificity; Thermal denaturation

Indexed keywords


EID: 18844431101     PISSN: 09199268     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1444-2906.2005.00978.x     Document Type: Article
Times cited : (26)

References (26)
  • 1
    • 0000922902 scopus 로고
    • Studies on the proteins of fish skeletal muscle. 7. Denaturation and aggregation of cod myosin
    • Connell JJ. 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
  • 2
    • 85007981637 scopus 로고
    • Studies on muscle protein of fish III. Inhibition by sorbitol and sucrose on the denaturation of carp actomyosin during frozen storage
    • Arai K, Takahashi H, Saito T. Studies on muscle protein of fish III. Inhibition by sorbitol and sucrose on the denaturation of carp actomyosin during frozen storage. Nippon Suisan Gakkaishi 1970; 36: 226-236.
    • (1970) Nippon Suisan Gakkaishi , vol.36 , pp. 226-236
    • Arai, K.1    Takahashi, H.2    Saito, T.3
  • 3
    • 0017158009 scopus 로고
    • Light chains of carp and pike skeletal muscle myosin. Isolation and characterization of the most anodic light chain on alkaline pH electrophoresis
    • Focant B, Huriaux F. Light chains of carp and pike skeletal muscle myosin. Isolation and characterization of the most anodic light chain on alkaline pH electrophoresis. FEBS Lett. 1976; 65: 16-19.
    • (1976) FEBS Lett. , vol.65 , pp. 16-19
    • Focant, B.1    Huriaux, F.2
  • 4
    • 84998225198 scopus 로고
    • Comparative studies on biochemical properties of myosins from frozen muscles of marine fishes
    • Kimura I, Murozuka T, Arai K. Comparative studies on biochemical properties of myosins from frozen muscles of marine fishes. Nippon Suisan Gakkaishi 1977; 43: 315-321.
    • (1977) Nippon Suisan Gakkaishi , vol.43 , pp. 315-321
    • Kimura, I.1    Murozuka, T.2    Arai, K.3
  • 5
    • 85008038649 scopus 로고
    • Relative thermo-stabilities of Ca-ATPase of myosin and actomyosin from tilapia and rabbit
    • Murozuka T, Takashi R, Arai K. Relative thermo-stabilities of Ca-ATPase of myosin and actomyosin from tilapia and rabbit. Nippon Suisan Gakkaishi 1976; 42: 57-63.
    • (1976) Nippon Suisan Gakkaishi , vol.42 , pp. 57-63
    • Murozuka, T.1    Takashi, R.2    Arai, K.3
  • 6
    • 18844431564 scopus 로고
    • Purification and thermo-stability of myosin Ca-ATPase from the frozen muscle of yellowfin tuna
    • Murozuka T, Arai K. Purification and thermo-stability of myosin Ca-ATPase from the frozen muscle of yellowfin tuna. Nippon Suisan Gakkaishi 1976; 42: 65-70.
    • (1976) Nippon Suisan Gakkaishi , vol.42 , pp. 65-70
    • Murozuka, T.1    Arai, K.2
  • 7
    • 0015654734 scopus 로고
    • The effect of environmental temperture on the properties of myofibrillar adenosine triphosphatase from various species of fish
    • Johnston IA, Freason N, Golberg G. The effect of environmental temperture on the properties of myofibrillar adenosine triphosphatase from various species of fish. Biochem. J. 1973; 133: 735-738.
    • (1973) Biochem. J. , vol.133 , pp. 735-738
    • Johnston, I.A.1    Freason, N.2    Golberg, G.3
  • 8
    • 85008030175 scopus 로고
    • Thermostability of fish myofibrillar Ca-ATPase and adaptation to enviromental temperature
    • Hashimoto A, Kobayashi A, Arai K. Thermostability of fish myofibrillar Ca-ATPase and adaptation to enviromental temperature. Nippon Suisan Gakkaishi 1982; 48: 671-684.
    • (1982) Nippon Suisan Gakkaishi , vol.48 , pp. 671-684
    • Hashimoto, A.1    Kobayashi, A.2    Arai, K.3
  • 10
    • 0024605313 scopus 로고
    • Thermal unfolding of myosin rod and light meromyosin. Circular dichroism and tryptophan fluorescence studies
    • King L, Lehrer SS. Thermal unfolding of myosin rod and light meromyosin. Circular dichroism and tryptophan fluorescence studies. Biochemistry 1989; 28: 3498-3502.
    • (1989) Biochemistry , vol.28 , pp. 3498-3502
    • King, L.1    Lehrer, S.S.2
  • 11
    • 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
  • 12
    • 0001460366 scopus 로고    scopus 로고
    • Oligomerization of carp myosin which retains its ATPase activity
    • Kato S, Koseki H, Konno K. Oligomerization of carp myosin which retains its ATPase activity. Fish. Sci. 1996; 62: 985-989.
    • (1996) Fish. Sci. , vol.62 , pp. 985-989
    • Kato, S.1    Koseki, H.2    Konno, K.3
  • 13
    • 0033789561 scopus 로고    scopus 로고
    • Early structual changes in myosin rod upon heating of carp myofibrils
    • Konno K, Yamamoto T, Takahashi M, Kato S. Early structual changes in myosin rod upon heating of carp myofibrils. J. Agric. Food Chem. 2000; 48: 4905-4909.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 4905-4909
    • Konno, K.1    Yamamoto, T.2    Takahashi, M.3    Kato, S.4
  • 14
    • 0036006643 scopus 로고    scopus 로고
    • Role of neck region in the thermal aggregation of myosin
    • Tazawa T, Kato S, Katoh T, Konno K. Role of neck region in the thermal aggregation of myosin. J. Agric. Food Chem. 2002; 50: 196-202.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 196-202
    • Tazawa, T.1    Kato, S.2    Katoh, T.3    Konno, K.4
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 85008121459 scopus 로고
    • Effect of neutral salts on thermal denaturation of myofibrillar Ca-ATPase of fish
    • Wakameda A, Nozawa S, Arai K. Effect of neutral salts on thermal denaturation of myofibrillar Ca-ATPase of fish. Nippon Suisan Gakkaishi 1983; 49: 237-243.
    • (1983) Nippon Suisan Gakkaishi , vol.49 , pp. 237-243
    • Wakameda, A.1    Nozawa, S.2    Arai, K.3
  • 17
    • 0036776140 scopus 로고    scopus 로고
    • Heat-induced structural changes and aggregation of walleye pollack myosin in the light meromyosin region
    • Higuchi T, Ojima T, Nishita K. Heat-induced structural changes and aggregation of walleye pollack myosin in the light meromyosin region. Fish. Sci. 2002; 68: 1145-1150.
    • (2002) Fish. Sci. , vol.68 , pp. 1145-1150
    • Higuchi, T.1    Ojima, T.2    Nishita, K.3
  • 18
    • 0000543143 scopus 로고    scopus 로고
    • Reversibility of unfolding of walleye pollack light meromyosin by heat-treatment
    • Ojima T, Higuchi T, Nishita K. Reversibility of unfolding of walleye pollack light meromyosin by heat-treatment. Fish. Sci. 1999; 65: 459-465.
    • (1999) Fish. Sci. , vol.65 , pp. 459-465
    • Ojima, T.1    Higuchi, T.2    Nishita, K.3
  • 19
    • 85008137505 scopus 로고
    • Chymotryptic digestibility of carp myosin as a probe of structure
    • Kato S, Konno K. Chymotryptic digestibility of carp myosin as a probe of structure. Nippon Suisan Gakkaishi 1990; 56: 1877-1883.
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 1877-1883
    • Kato, S.1    Konno, K.2
  • 20
    • 85008122367 scopus 로고
    • The amount of actin dissociated from myosin B in the presence of NaCl
    • Wakameda A, Arai K. The amount of actin dissociated from myosin B in the presence of NaCl. Nippon Suisan Gakkaishi 1985; 51: 497-502.
    • (1985) Nippon Suisan Gakkaishi , vol.51 , pp. 497-502
    • Wakameda, A.1    Arai, K.2
  • 21
    • 85008271904 scopus 로고
    • Preparation and biochemical properties of subfragment-1 from dorsal muscle of carp (Cyprinus carpio)
    • Ikariya T, Kimura I, Arai K. Preparation and biochemical properties of subfragment-1 from dorsal muscle of carp (Cyprinus carpio). Nippon Suisan Gakkaishi 1981; 47: 947-955.
    • (1981) Nippon Suisan Gakkaishi , vol.47 , pp. 947-955
    • Ikariya, T.1    Kimura, I.2    Arai, K.3
  • 23
    • 84987313409 scopus 로고
    • Suppression of thermal denaturation of myosin subfragment-1 of Alaska pollack (Thergra chalcogramma) by sorbitol and accelerated inactivation by pyrophosphate
    • Konno K. Suppression of thermal denaturation of myosin subfragment-1 of Alaska pollack (Thergra chalcogramma) by sorbitol and accelerated inactivation by pyrophosphate. J. Food Sci. 1992; 57: 261-264.
    • (1992) J. Food Sci. , vol.57 , pp. 261-264
    • Konno, K.1
  • 25
    • 85006124320 scopus 로고
    • Thermo-stabilities of synthetic actomyosins in various combinations of myosin and actin from fish, scallop, and rabbit muscles
    • Yamashita Y, Arai K, Nishita K. Thermo-stabilities of synthetic actomyosins in various combinations of myosin and actin from fish, scallop, and rabbit muscles. Nippon Suisan Gakkaishi 1978; 44: 485-489.
    • (1978) Nippon Suisan Gakkaishi , vol.44 , pp. 485-489
    • Yamashita, Y.1    Arai, K.2    Nishita, K.3
  • 26
    • 0024259522 scopus 로고
    • Thick filaments of fish myosin and its actin-activated Mg-ATPase activity
    • Matsuura M, Konno K, Arai K. Thick filaments of fish myosin and its actin-activated Mg-ATPase activity. Comp. Biochem. Physiol. 1988; 90B: 803-808.
    • (1988) Comp. Biochem. Physiol. , vol.90 B , pp. 803-808
    • Matsuura, M.1    Konno, K.2    Arai, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.