메뉴 건너뛰기




Volumn 74, Issue 4, 2008, Pages 921-934

cDNA cloning and complete primary structures of myosin heavy chains from brushtooth lizardfish Saurida undosquamis and wanieso lizardfish S. wanieso fast skeletal muscles

Author keywords

Brushtooth lizardfish; cDNA; Fast skeletal muscle; Myosin heavy chain; Primary structure; Wanieso lizardfish

Indexed keywords

GENYONEMUS LINEATUS; POLLACHIUS POLLACHIUS; SAURIDA UNDOSQUAMIS; STIZOSTEDION VITREUM;

EID: 49249113098     PISSN: 09199268     EISSN: 14442906     Source Type: Journal    
DOI: 10.1111/j.1444-2906.2008.01607.x     Document Type: Article
Times cited : (5)

References (31)
  • 1
    • 0010727621 scopus 로고
    • Muscle development and contractile proteins
    • In: Bechtel, P.J., ed. Academic Press, Orland.
    • Bechtel PJ. Muscle development and contractile proteins. In : Bechtel PJ, ed. Muscle as Food. Academic Press, Orland. 1986 1 35.
    • (1986) Muscle As Food. , pp. 1-35
    • Bechtel, P.J.1
  • 3
    • 0014693726 scopus 로고
    • Substructure of the myosin molecule. I. Subfragments of myosin by enzymatic degradation
    • Lowey S, Slayter HS, Weeds AG, Baker H. Substructure of the myosin molecule. I. Subfragments of myosin by enzymatic degradation. J. Mol. Biol. 1969 42 : 1 29.
    • (1969) J. Mol. Biol. , vol.42 , pp. 1-29
    • Lowey, S.1    Slayter, H.S.2    Weeds, A.G.3    Baker, H.4
  • 4
    • 0000724738 scopus 로고
    • The relative stabilities of the skeletal-muscle myosins of some animals
    • Connell JJ. The relative stabilities of the skeletal-muscle myosins of some animals. Biochem. J. 1961 80 : 503 509.
    • (1961) Biochem. J. , vol.80 , pp. 503-509
    • Connell, J.J.1
  • 5
    • 0015654734 scopus 로고
    • The effects of environmental temperature on the properties of myofibrillar adenosine triphosphatase from various species of fish
    • Johnston IA, Frearson N, Goldspink G. The effects of environmental temperature 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    Frearson, N.2    Goldspink, G.3
  • 6
    • 18744369369 scopus 로고    scopus 로고
    • CDNA cloning of myosin heavy chain from white croaker fast skeletal muscle and characterization of its complete primary structure
    • Yoon HS, Kakinuma M, Hirayama Y, Yamamoto T, Watabe S. cDNA cloning of myosin heavy chain from white croaker fast skeletal muscle and characterization of its complete primary structure. Fish Sci. 2000 66 : 1163 1171.
    • (2000) Fish Sci. , vol.66 , pp. 1163-1171
    • Yoon, H.S.1    Kakinuma, M.2    Hirayama, Y.3    Yamamoto, T.4    Watabe, S.5
  • 7
    • 0038691746 scopus 로고    scopus 로고
    • Differences in polymer formation through disulfide bonding of recombinant light meromyosin between white croaker and walleye pollack and their possible relation to species-specific differences in thermal unfolding
    • Fukushima H, Yoon HS, Watabe S. Differences in polymer formation through disulfide bonding of recombinant light meromyosin between white croaker and walleye pollack and their possible relation to species-specific differences in thermal unfolding. J. Agric. Food Chem. 2003 51 : 4089 4095.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 4089-4095
    • Fukushima, H.1    Yoon, H.S.2    Watabe, S.3
  • 8
    • 0038573664 scopus 로고    scopus 로고
    • Thermal effects on the fast skeletal myosins from Alaska pollack, white croaker, and rabbit in relation to gel formation
    • Fukushima H, Satoh Y, Nakaya S, Watabe S. Thermal effects on the fast skeletal myosins from Alaska pollack, white croaker, and rabbit in relation to gel formation. J. Food Sci. 2003 68 : 1573 1577.
    • (2003) J. Food Sci. , vol.68 , pp. 1573-1577
    • Fukushima, H.1    Satoh, Y.2    Nakaya, S.3    Watabe, S.4
  • 9
    • 28444467468 scopus 로고    scopus 로고
    • Rheological properties of fast skeletal myosin rod and light meromyosin from walleye pollack and white croaker: Contribution of myosin fragments to thermal gel formation
    • Fukushima H, Satoh Y, Yoon HS, Togashi M, Nakaya M, Watabe S. Rheological properties of fast skeletal myosin rod and light meromyosin from walleye pollack and white croaker: contribution of myosin fragments to thermal gel formation. J. Agric. Food Chem. 2005 53 : 9193 9198.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 9193-9198
    • Fukushima, H.1    Satoh, Y.2    Yoon, H.S.3    Togashi, M.4    Nakaya, M.5    Watabe, S.6
  • 10
    • 33745037483 scopus 로고    scopus 로고
    • Characterization of fast skeletal myosin from white croaker in comparison with that from walleye pollack
    • Satoh Y, Nakaya M, Ochiai Y, Watabe S. Characterization of fast skeletal myosin from white croaker in comparison with that from walleye pollack. Fish Sci. 2006 72 : 646 655.
    • (2006) Fish Sci. , vol.72 , pp. 646-655
    • Satoh, Y.1    Nakaya, M.2    Ochiai, Y.3    Watabe, S.4
  • 11
    • 0000990096 scopus 로고    scopus 로고
    • Determination of primary structure of heavy meromyosin region of walleye pollack myosin heavy chain by cDNA cloning
    • Ojima T, Kawashima N, Inoue A, Amauchi A, Togashi M, Watabe S, Nishita K. Determination of primary structure of heavy meromyosin region of walleye pollack myosin heavy chain by cDNA cloning. Fish Sci. 1998 64 : 812 819.
    • (1998) Fish Sci. , vol.64 , pp. 812-819
    • Ojima, T.1    Kawashima, N.2    Inoue, A.3    Amauchi, A.4    Togashi, M.5    Watabe, S.6    Nishita, K.7
  • 12
    • 0001136664 scopus 로고    scopus 로고
    • CDNA cloning of myosin rod and complete primary structure of myosin heavy chain of walleye pollack fast skeletal muscle
    • Togashi M, Kakinuma M, Hirayama Y, Fukushima H, Watabe S, Ojima T, Nishita K. cDNA cloning of myosin rod and complete primary structure of myosin heavy chain of walleye pollack fast skeletal muscle. Fish Sci. 2000 66 : 349 357.
    • (2000) Fish Sci. , vol.66 , pp. 349-357
    • Togashi, M.1    Kakinuma, M.2    Hirayama, Y.3    Fukushima, H.4    Watabe, S.5    Ojima, T.6    Nishita, K.7
  • 13
    • 0037077363 scopus 로고    scopus 로고
    • Differential scanning calorimetry and circular dichroism spectrophotometry of walleye pollack myosin and light meromyosin
    • Togashi M, Kakinuma M, Nakaya M, Ooi T, Watabe S. Differential scanning calorimetry and circular dichroism spectrophotometry of walleye pollack myosin and light meromyosin. J. Agric. Food Chem. 2002 50 : 4803 4811.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 4803-4811
    • Togashi, M.1    Kakinuma, M.2    Nakaya, M.3    Ooi, T.4    Watabe, S.5
  • 14
    • 0346875597 scopus 로고
    • On board treatment of lizardfish as raw material for fish jelly products
    • Nozaki Y, Yamamoto T, Tabata Y. On board treatment of lizardfish as raw material for fish jelly products. Nippon Suisan Gakkaishi 1986 52 : 1565 1572.
    • (1986) Nippon Suisan Gakkaishi , vol.52 , pp. 1565-1572
    • Nozaki, Y.1    Yamamoto, T.2    Tabata, Y.3
  • 15
    • 0042303840 scopus 로고    scopus 로고
    • Effect of proteolytic squid protein hydrolysate on the state of water and dehydration-induced denaturation of lizardfish myosin
    • Hossain MA, Ishihara T, Hara K, Osatomi K, Khan MAA, Nozaki Y. Effect of proteolytic squid protein hydrolysate on the state of water and dehydration-induced denaturation of lizardfish myosin. J. Agric. Food Chem. 2003 51 : 4769 4774.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 4769-4774
    • Hossain, M.A.1    Ishihara, T.2    Hara, K.3    Osatomi, K.4    Khan, M.A.A.5    Nozaki, Y.6
  • 16
    • 33645736470 scopus 로고    scopus 로고
    • Effect of fish protein hydrolysate on the gel-forming ability, state of water, and denaturation of lizardfish (Saurida wanieso) surimi during frozen storage
    • Khan MAA, Hossain MA, Ishihara T, Hara K, Osatomi K, Nozaki Y. Effect of fish protein hydrolysate on the gel-forming ability, state of water, and denaturation of lizardfish (Saurida wanieso) surimi during frozen storage. Trans. JSRAE 2003 20 : 185 191.
    • (2003) Trans. JSRAE , vol.20 , pp. 185-191
    • Khan, M.A.A.1    Hossain, M.A.2    Ishihara, T.3    Hara, K.4    Osatomi, K.5    Nozaki, Y.6
  • 17
    • 0012216869 scopus 로고    scopus 로고
    • Molecular phylogeny of Asian freshwater and marine stingrays based on the DNA nucleotide and deduced amino acid sequences of the cytochrome b gene
    • Sezaki K, Begum RA, Wongrat P, Srivastava MP, Sri Kantha S, Ishihara H, Tanaka S, Taniuchi T, Watabe S. Molecular phylogeny of Asian freshwater and marine stingrays based on the DNA nucleotide and deduced amino acid sequences of the cytochrome b gene. Fish Sci. 1999 65 : 563 570.
    • (1999) Fish Sci. , vol.65 , pp. 563-570
    • Sezaki, K.1    Begum, R.A.2    Wongrat, P.3    Srivastava, M.P.4    Sri Kantha, S.5    Ishihara, H.6    Tanaka, S.7    Taniuchi, T.8    Watabe, S.9
  • 18
    • 0001829453 scopus 로고    scopus 로고
    • Nucleic acids II. the polymerase chain reaction
    • In: Hillis, D.M., Moritz, C., Mable, B.K., eds. Sinauer Associates, Massachusetts.
    • Palumbi SR. Nucleic acids II. the polymerase chain reaction. In : Hillis DM, Moritz C, Mable BK, eds. Molecular Systematics, 2nd edn. Sinauer Associates, Massachusetts. 1996 205 247.
    • (1996) Molecular Systematics, 2nd Edn. , pp. 205-247
    • Palumbi, S.R.1
  • 19
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson DJ, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 1997 25 : 4876 4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, D.J.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 20
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S, Tamura K, Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinform. 2004 5 : 150 163.
    • (2004) Brief. Bioinform. , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 21
    • 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, Hirayama Y, Kikuchi K, Kakinuma M, Watabe S. cDNA cloning of myosin heavy chain isoforms from carp fast skeletal muscle and their gene expression associated with temperature acclimation. J. Exp. Biol. 1997 200 : 27 34.
    • (1997) J. Exp. Biol. , vol.200 , pp. 27-34
    • Imai, J.1    Hirayama, Y.2    Kikuchi, K.3    Kakinuma, M.4    Watabe, S.5
  • 22
    • 0030909175 scopus 로고    scopus 로고
    • Structural differences in the crossbridge head of temperature-associated myosin subfragment-1 isoforms from carp fast skeletal muscle
    • Hirayama Y, Watabe S. Structural differences in the crossbridge head of temperature-associated myosin subfragment-1 isoforms from carp fast skeletal muscle. Eur. J. Biochem. 1997 246 : 380 387.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 380-387
    • Hirayama, Y.1    Watabe, S.2
  • 23
    • 0032510769 scopus 로고    scopus 로고
    • Dictyostelium myosin 25-50K loop substitutions specifically affect ADP release rates
    • Murphy CT, Spudich JA. Dictyostelium myosin 25-50K loop substitutions specifically affect ADP release rates. Biochemistry 1998 37 : 6738 6744.
    • (1998) Biochemistry , vol.37 , pp. 6738-6744
    • Murphy, C.T.1    Spudich, J.A.2
  • 24
    • 0028354078 scopus 로고
    • Enzymatic activities correlate with chimeric substitutions at the actin binding face of myosin
    • Uyeda TQP, Ruppel KM, Spudich JA. Enzymatic activities correlate with chimeric substitutions at the actin binding face of myosin. Nature 1994 368 : 567 569.
    • (1994) Nature , vol.368 , pp. 567-569
    • Uyeda, T.Q.P.1    Ruppel, K.M.2    Spudich, J.A.3
  • 25
    • 0034607138 scopus 로고    scopus 로고
    • Structure-function relationships of the two surface loops of myosin heavy chain isoforms from thermally acclimated carp
    • Hirayama Y, Sutoh K, Watabe S. Structure-function relationships of the two surface loops of myosin heavy chain isoforms from thermally acclimated carp. Biochem. Biophys. Res. Commun. 2000 269 : 237 241.
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 237-241
    • Hirayama, Y.1    Sutoh, K.2    Watabe, S.3
  • 26
    • 0025826377 scopus 로고
    • The primary structure of skeletal muscle myosin heavy chain. IV. Sequence of the rod, and the complete 1,938-residue sequence of the heavy chain
    • Maita T, Yajima E, Nagata S, Miyanishi T, Nakayama S, Matsuda G. The primary structure of skeletal muscle myosin heavy chain. IV. Sequence of the rod, and the complete 1,938-residue sequence of the heavy chain. J. Biochem. 1991 110 : 75 87.
    • (1991) J. Biochem. , vol.110 , pp. 75-87
    • Maita, T.1    Yajima, E.2    Nagata, S.3    Miyanishi, T.4    Nakayama, S.5    Matsuda, G.6
  • 27
    • 0033665512 scopus 로고    scopus 로고
    • Characterization of red and white muscle myosin heavy chain gene coding sequences from Antarctic and tropical fish
    • Gauvry L, Ennion S, Ettelaie C, Goldspink G. Characterization of red and white muscle myosin heavy chain gene coding sequences from Antarctic and tropical fish. Comp. Biochem. Physiol. B 2000 127 : 575 588.
    • (2000) Comp. Biochem. Physiol. B , vol.127 , pp. 575-588
    • Gauvry, L.1    Ennion, S.2    Ettelaie, C.3    Goldspink, G.4
  • 29
    • 0019975166 scopus 로고
    • Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle
    • McLachlan AD, Karn J. Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature 1982 299 : 803 808.
    • (1982) Nature , vol.299 , pp. 803-808
    • McLachlan, A.D.1    Karn, J.2
  • 30
    • 0036791176 scopus 로고    scopus 로고
    • Primary structure of myosin heavy chain from fast skeletal muscle of chum salmon Oncorhynchus keta
    • Iwami Y, Ojima T, Inoue A, Nishita K. Primary structure of myosin heavy chain from fast skeletal muscle of chum salmon Oncorhynchus keta. Comp. Biochem. Physiol. B 2002 133 : 257 267.
    • (2002) Comp. Biochem. Physiol. B , vol.133 , pp. 257-267
    • Iwami, Y.1    Ojima, T.2    Inoue, A.3    Nishita, K.4
  • 31
    • 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. Differential scanning calorimetry of light meromyosin fragments having various lengths of carp fast skeletal muscle isoforms. J. Biochem. 2000 128 : 11 20.
    • (2000) J. Biochem. , vol.128 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.