메뉴 건너뛰기




Volumn 71, Issue 1, 2006, Pages

Seasonal expression of 2 types of myosin with different thermostability in silver carp muscle (Hypophthalmichthys molitrix)

Author keywords

Ca ATPase activity; Myofibrils; Myosin; Silver carp; Thermostability

Indexed keywords

CYPRINUS CARPIO; HYPOPHTHALMICHTHYS MOLITRIX; HYPOPHTHALMICHTHYS NOBILIS;

EID: 32444434067     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2006.tb12386.x     Document Type: Article
Times cited : (21)

References (27)
  • 1
    • 32444437225 scopus 로고    scopus 로고
    • Beijing; China: Agricultural Publishing Co.
    • [CFYEC] China Fisheries Yearbook Edit Committee. 2004. Yearbook of China fisheries 2003. Beijing; China: Agricultural Publishing Co. 220 p.
    • (2004) Yearbook of China Fisheries 2003
  • 2
    • 0001340438 scopus 로고    scopus 로고
    • Freeze denaturation of carp myofibrils compared with thermal denaturation
    • Azuma Y, Konno K. 1998. Freeze denaturation of carp myofibrils compared with thermal denaturation. Fisheries Sci 64(2):287-90.
    • (1998) Fisheries Sci , vol.64 , Issue.2 , pp. 287-290
    • Azuma, Y.1    Konno, K.2
  • 3
    • 21544433786 scopus 로고    scopus 로고
    • Effects of heating methods on gel-forming ability of silver carp (Hypophthalmichthys molitrix) surimi
    • Cao Y, Cheng Y, Wang X, Chen S. 2003. Effects of heating methods on gel-forming ability of silver carp (Hypophthalmichthys molitrix) surimi. J Shanghai Fish Univ 12:78-85.
    • (2003) J Shanghai Fish Univ , vol.12 , pp. 78-85
    • Cao, Y.1    Cheng, Y.2    Wang, X.3    Chen, S.4
  • 4
    • 21544476457 scopus 로고    scopus 로고
    • Effect of freshness for iced silver carp on gel formation
    • Chen S, Wang X, Zhou L, Fukuda Y. 2000. Effect of freshness for iced silver carp on gel formation. J. Shanghai Fish. Univ 9(1):45-50.
    • (2000) J Shanghai Fish Univ , vol.9 , Issue.1 , pp. 45-50
    • Chen, S.1    Wang, X.2    Zhou, L.3    Fukuda, Y.4
  • 6
    • 0038573664 scopus 로고    scopus 로고
    • Thermal effects on fast skeletal myosins from walleye pollack, white croaker and rabbit in relation to gel formation
    • Fukushima H, Satoh Y, Nakaya M, Ishizaki S, Watabe S. 2003. Thermal effects on fast skeletal myosins from walleye pollack, white croaker and rabbit in relation to gel formation. J. Food Sci 68(5):1573-7.
    • (2003) J Food Sci , vol.68 , Issue.5 , pp. 1573-1577
    • Fukushima, H.1    Satoh, Y.2    Nakaya, M.3    Ishizaki, S.4    Watabe, S.5
  • 7
    • 85010179866 scopus 로고
    • ATPase activity and thermostability of actomyosins from thermally acclimated carp
    • Guo XF, Watabe S. 1993. ATPase activity and thermostability of actomyosins from thermally acclimated carp. Nippon Suisan Gakkaishi 59:363-9.
    • (1993) Nippon Suisan Gakkaishi , vol.59 , pp. 363-369
    • Guo, X.F.1    Watabe, S.2
  • 8
    • 85008030175 scopus 로고
    • Thermostability of fish myofibrillar CaATPase and adaptation to environmental temperature
    • Hashimoto A, Kobayashi A, Arai K. 1982. Thermostability of fish myofibrillar CaATPase and adaptation to environmental temperature. Nippon Suisan Gakkaishi 48(5):671-84.
    • (1982) Nippon Suisan Gakkaishi , vol.48 , Issue.5 , pp. 671-684
    • Hashimoto, A.1    Kobayashi, A.2    Arai, K.3
  • 9
    • 0025113856 scopus 로고
    • Changes in carp myosin ATPase induced by temperature acclimation
    • Hwang GC, Watabe S, Hashimoto K. 1990. Changes in carp myosin ATPase induced by temperature acclimation. J Comp Physiol B 160:233-9.
    • (1990) J Comp Physiol B , vol.160 , pp. 233-239
    • Hwang, G.C.1    Watabe, S.2    Hashimoto, K.3
  • 10
    • 0031019058 scopus 로고    scopus 로고
    • cDNA cloning of myosin heavy chain isoforms from carp fast skeletal muscle and their gene expression associated with temperature acclimation
    • Imai J, Hrayama Y, Kikuchi K, Kakinuma M, Watabe S. 1997. cDNA cloning of myosin heavy chain isoforms from carp fast skeletal muscle and their gene expression associated with temperature acclimation. J Exp Biol 200:27-34.
    • (1997) J Exp Biol , vol.200 , pp. 27-34
    • Imai, J.1    Hrayama, Y.2    Kikuchi, K.3    Kakinuma, M.4    Watabe, S.5
  • 11
    • 0012388642 scopus 로고
    • Effect of temperature on the rate for the setting of meat pastes from Alaska pollack, white croaker and tilapia
    • Kato N, Hashimoto A, Nozaki H, Arai K. 1984. Effect of temperature on the rate for the setting of meat pastes from Alaska pollack, white croaker and tilapia. Nippon Suisan Gakkaishi 50(12):2103-8.
    • (1984) Nippon Suisan Gakkaishi , vol.50 , Issue.12 , pp. 2103-2108
    • Kato, N.1    Hashimoto, A.2    Nozaki, H.3    Arai, K.4
  • 12
    • 21144475288 scopus 로고
    • Myosin extractability as a sensitive probe for the thermal denaturation of carp myofibrils
    • Koseki H, Kato S, Konno K. 1993. Myosin extractability as a sensitive probe for the thermal denaturation of carp myofibrils. Nippon Suisan Gakkaishi 59(3):515-8.
    • (1993) Nippon Suisan Gakkaishi , vol.59 , Issue.3 , pp. 515-518
    • Koseki, H.1    Kato, S.2    Konno, K.3
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 85008095850 scopus 로고
    • Cooperative effect of carboxylic acid and sugar against freeze denaturation of fish myofibrillar protein
    • Matsumoto I, Arai K. 1987. Cooperative effect of carboxylic acid and sugar against freeze denaturation of fish myofibrillar protein. Nippon Suisan Gakkaishi 53(12):2187-93.
    • (1987) Nippon Suisan Gakkaishi , vol.53 , Issue.12 , pp. 2187-2193
    • Matsumoto, I.1    Arai, K.2
  • 15
    • 7544243302 scopus 로고    scopus 로고
    • Effect of silver carp Hypophthalmichthys molitrix and freshwater mussel Elliptic complanata filtration on the phytoplankton community of partitioned aquaculture system
    • Mueller CR, Eversole AG, Turker H; Brune DE. 2004. Effect of silver carp Hypophthalmichthys molitrix and freshwater mussel Elliptic complanata filtration on the phytoplankton community of partitioned aquaculture system. J. World Aquacult Soc 35(3):372-82.
    • (2004) J World Aquacult Soc , vol.35 , Issue.3 , pp. 372-382
    • Mueller, C.R.1    Eversole, A.G.2    Turker, H.3    Brune, D.E.4
  • 16
    • 0015218407 scopus 로고
    • Biochemical studies of the interaction of the tropomyosin-troponin complexes with actin and the proteolytic fragments of myosin
    • Spudich JA, Watt S. 1971. Biochemical studies of the interaction of the tropomyosin-troponin complexes with actin and the proteolytic fragments of myosin. J Biol Chem 246:4866-71.
    • (1971) J Biol Chem , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 17
    • 18844431101 scopus 로고    scopus 로고
    • Species-specific thermal denaturation pattern of fish myosin when heated as myofibrils as studied by myosin subfragment-1 and rod denaturation rates
    • Takahashi M, Yamamoto T, Kato S, Konno K. 2005. Species-specific thermal denaturation pattern of fish myosin when heated as myofibrils as studied by myosin subfragment-1 and rod denaturation rates. Fisheries Sci 71(2):405-13.
    • (2005) Fisheries Sci , vol.71 , Issue.2 , pp. 405-413
    • Takahashi, M.1    Yamamoto, T.2    Kato, S.3    Konno, K.4
  • 18
    • 0346158702 scopus 로고    scopus 로고
    • A new purification method of G-actin extracted from the acetone-dried myofibril-powder using ammonium sulfate fractionation. A comparison with the conventional G-actin and high-salt sensitivity
    • Torigai M, Konno K. 1997. A new purification method of G-actin extracted from the acetone-dried myofibril-powder using ammonium sulfate fractionation. A comparison with the conventional G-actin and high-salt sensitivity. Fisheries Sci 63(3):397-402.
    • (1997) Fisheries Sci , vol.63 , Issue.3 , pp. 397-402
    • Torigai, M.1    Konno, K.2
  • 19
    • 85006168078 scopus 로고
    • Biochemical studies on myofibrils of fish: Thermostability of fish species
    • Uchiyama H, Katoh N, Kudo Y, Arai K. 1978. Biochemical studies on myofibrils of fish: Thermostability of fish species. Nippon Suisan Gakkaishi 44(5):491-8.
    • (1978) Nippon Suisan Gakkaishi , vol.44 , Issue.5 , pp. 491-498
    • Uchiyama, H.1    Katoh, N.2    Kudo, Y.3    Arai, K.4
  • 20
    • 85008122367 scopus 로고
    • The amount of actin dissociated from myosin B in the presence of NaCl
    • Wakameda A, Arai K. 1985. The amount of actin dissociated from myosin B in the presence of NaCl. Nippon Suisan Gakkaishi 51(3):497-502.
    • (1985) Nippon Suisan Gakkaishi , vol.51 , Issue.3 , pp. 497-502
    • Wakameda, A.1    Arai, K.2
  • 21
    • 85008537135 scopus 로고
    • Dissociation of carp myosin B into actin and myosin in the presence of a high concentration of NaCl
    • Wakameda A, Arai K. 1986. Dissociation of carp myosin B into actin and myosin in the presence of a high concentration of NaCl. Nippon Suisan Gakkaishi 52(3):293-300.
    • (1986) Nippon Suisan Gakkaishi , vol.52 , Issue.3 , pp. 293-300
    • Wakameda, A.1    Arai, K.2
  • 22
    • 0036195333 scopus 로고    scopus 로고
    • Acceptability comparison of kamaboko gels derived from silver carp surimi and from walleye Pollack surimi between the Chinese and Japanese
    • Wang X, Hirata T, Fukuda Y, Kinoshita M, Sakakuchi M. 2002. Acceptability comparison of kamaboko gels derived from silver carp surimi and from walleye Pollack surimi between the Chinese and Japanese. Fisheries Sci 68(1):165-9.
    • (2002) Fisheries Sci , vol.68 , Issue.1 , pp. 165-169
    • Wang, X.1    Hirata, T.2    Fukuda, Y.3    Kinoshita, M.4    Sakakuchi, M.5
  • 23
    • 5844289146 scopus 로고    scopus 로고
    • Seasonal effect on thermostability of myofibrillar Ca-ATPase in Freshwater fish muscle
    • Wang Z, Hu F, Luo Z. 1997. Seasonal effect on thermostability of myofibrillar Ca-ATPase in Freshwater fish muscle. J Aquat Food Prod Technol 6(2):5-15.
    • (1997) J Aquat Food Prod Technol , vol.6 , Issue.2 , pp. 5-15
    • Wang, Z.1    Hu, F.2    Luo, Z.3
  • 24
    • 0031461886 scopus 로고    scopus 로고
    • Carp expresses fast skeletal myosin isoforms with altered motor functions and structural stabilities to compensate for changes in environmental temperatures
    • Watabe S, Hirayama Y, Nakaya M, Kakinuma M, Kikuchi K, Guo X, Kanon S, Chaen S, Ooi T. 1998. Carp expresses fast skeletal myosin isoforms with altered motor functions and structural stabilities to compensate for changes in environmental temperatures. J Therm Biol 22:375-90.
    • (1998) J Therm Biol , vol.22 , pp. 375-390
    • Watabe, S.1    Hirayama, Y.2    Nakaya, M.3    Kakinuma, M.4    Kikuchi, K.5    Guo, X.6    Kanon, S.7    Chaen, S.8    Ooi, T.9
  • 26
    • 21544445284 scopus 로고    scopus 로고
    • Comparison of gel-forming properties of silver carp (Hypophthalmichthys molitrix) surimi prepared in different seasons
    • Yuan C, Fukuda Y, Kaneniwa M, Chen Y, Cheng Y, Wang X, Konno K. 2005. Comparison of gel-forming properties of silver carp (Hypophthalmichthys molitrix) surimi prepared in different seasons. J Food Sci 70(5):326-31.
    • (2005) J Food Sci , vol.70 , Issue.5 , pp. 326-331
    • Yuan, C.1    Fukuda, Y.2    Kaneniwa, M.3    Chen, Y.4    Cheng, Y.5    Wang, X.6    Konno, K.7
  • 27
    • 85047677412 scopus 로고    scopus 로고
    • Fisheries in China: Progress, problems, and prospects
    • Zhong Y, Power G, 1997. Fisheries in China: progress, problems, and prospects. Can J Fish Aquat Sci 54:224-38.
    • (1997) Can J Fish Aquat Sci , vol.54 , pp. 224-238
    • Zhong, Y.1    Power, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.