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Volumn 21, Issue 4, 1999, Pages 287-301

Myofibrillar proteins in white muscle of the developing African catfish Heterobranchus longifilis (Siluriforms, Clariidae)

Author keywords

Development; Fish; Myosin heavy chain; Myosin light chain; Polyacrylamide gel electrophoresis; Tropomyosin; Troponin C; Troponin I; Troponin T

Indexed keywords

CLARIIDAE; HETEROBRANCHUS LONGIFILIS; SILURIFORMES;

EID: 0037783116     PISSN: 09201742     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1007835101472     Document Type: Article
Times cited : (14)

References (57)
  • 1
    • 0032921584 scopus 로고    scopus 로고
    • Sibling cannibalism among juvenile vundu under controlled conditions. I. Cannibalistic behaviour, prey selection and prey size selectivity
    • Baras, E. 1999. Sibling cannibalism among juvenile vundu under controlled conditions. I. Cannibalistic behaviour, prey selection and prey size selectivity. J. Fish Biol. 54: 82-105.
    • (1999) J. Fish Biol. , vol.54 , pp. 82-105
    • Baras, E.1
  • 2
    • 2342624398 scopus 로고
    • Myosin isoforms in white, red and pink muscles of the teleost sea bass (Dicentrarchus labrax L.)
    • Bassani, V. and Dalla Libera, L. 1991. Myosin isoforms in white, red and pink muscles of the teleost sea bass (Dicentrarchus labrax L.). BAM 1: 153-156.
    • (1991) BAM , vol.1 , pp. 153-156
    • Bassani, V.1    Dalla Libera, L.2
  • 3
    • 77956847788 scopus 로고
    • Locomotor muscle
    • Edited by W.S. Hoar and D.J. Randall. Academic Press, New York
    • Bone, Q. 1978. Locomotor muscle. In: Fish Physiology. Vol. 7, pp. 361-424. Edited by W.S. Hoar and D.J. Randall. Academic Press, New York.
    • (1978) Fish Physiology , vol.7 , pp. 361-424
    • Bone, Q.1
  • 4
    • 0000044945 scopus 로고
    • Influence of development and rearing temperature on the distribution, ultrastructure and myosin sub-unit composition of myotomal muscle-fibre types in the plaice Pleuronectes platessa
    • Brooks, S. and Johnston, I.A. 1993. Influence of development and rearing temperature on the distribution, ultrastructure and myosin sub-unit composition of myotomal muscle-fibre types in the plaice Pleuronectes platessa. Mar. Biol. 117: 501-513.
    • (1993) Mar. Biol. , vol.117 , pp. 501-513
    • Brooks, S.1    Johnston, I.A.2
  • 5
    • 0020643575 scopus 로고
    • 2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, with the cationic carbocyanine dye 'Stains-all'
    • 2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, with the cationic carbocyanine dye 'Stains-all'. J. Biol. Chem. 258: 11267-11273.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11267-11273
    • Campbell, K.P.1    MacLennan, D.H.2    Jorgensen, A.O.3
  • 6
    • 0025676113 scopus 로고
    • Myosin structure in the eel (Anguilla anguilla L.). Demonstration of three heavy chains in adult lateral muscle
    • Chanoine, C., Saadi, A., Guyot-Lenfant, M., Hebbrecht, C. and Gallien, C.L. 1990. Myosin structure in the eel (Anguilla anguilla L.). Demonstration of three heavy chains in adult lateral muscle. FEBS Lett. 277: 200-204.
    • (1990) FEBS Lett. , vol.277 , pp. 200-204
    • Chanoine, C.1    Saadi, A.2    Guyot-Lenfant, M.3    Hebbrecht, C.4    Gallien, C.L.5
  • 7
    • 0026606765 scopus 로고
    • White muscle differentiation in the eel (Anguilla anguilla L.): Changes in the myosin isoforms pattern and ATPase profile during post-metamorphic development
    • Chanoine, C., Guyot-Lenfant, M., El Attari, A., Saadi, A. and Gallien, C.L. 1992. White muscle differentiation in the eel (Anguilla anguilla L.): changes in the myosin isoforms pattern and ATPase profile during post-metamorphic development. Differentiation 49: 69-75.
    • (1992) Differentiation , vol.49 , pp. 69-75
    • Chanoine, C.1    Guyot-Lenfant, M.2    El Attari, A.3    Saadi, A.4    Gallien, C.L.5
  • 8
    • 0031430398 scopus 로고    scopus 로고
    • Isoform distribution of parvalbumins and of some myofibrillar proteins in adult and developing Chrysichthys auratus (Geoffroy St Hilaire, 1808) (Pisces, Claroteidae)
    • Chikou, A., Huriaux, F., Laleye, P., Vandewalle, P. and Focant, B. 1997. Isoform distribution of parvalbumins and of some myofibrillar proteins in adult and developing Chrysichthys auratus (Geoffroy St Hilaire, 1808) (Pisces, Claroteidae). Arch. Physiol. Biochem. 105: 611-617.
    • (1997) Arch. Physiol. Biochem. , vol.105 , pp. 611-617
    • Chikou, A.1    Huriaux, F.2    Laleye, P.3    Vandewalle, P.4    Focant, B.5
  • 9
    • 33751138851 scopus 로고
    • Developmental changes in the composition of myofibrillar proteins in the swimming muscles of Atlantic herring, Clupea harengus
    • Crockford, T. and Johnston, I.A. 1993. Developmental changes in the composition of myofibrillar proteins in the swimming muscles of Atlantic herring, Clupea harengus. Mar. Biol. 115: 15-22.
    • (1993) Mar. Biol. , vol.115 , pp. 15-22
    • Crockford, T.1    Johnston, I.A.2
  • 10
    • 0025836315 scopus 로고
    • Inter- and intra-specific variation in myosin light chain and troponin I composition in fast muscle fibres from two species of fish (Genus Oreochromis) which have different temperature-dependent contractile properties
    • Crockford, T., Wommack, K.E., Johnston, I.A., McAndrew, B.J., Mutungi, G. and Johnson, T.P. 1991. Inter- and intra-specific variation in myosin light chain and troponin I composition in fast muscle fibres from two species of fish (Genus Oreochromis) which have different temperature-dependent contractile properties. J. Muscle Res. Cell Motil. 12: 439-446.
    • (1991) J. Muscle Res. Cell Motil. , vol.12 , pp. 439-446
    • Crockford, T.1    Wommack, K.E.2    Johnston, I.A.3    McAndrew, B.J.4    Mutungi, G.5    Johnson, T.P.6
  • 11
    • 0022483072 scopus 로고
    • Type I, 2A and 2B myosin heavy chain electrophoretic analysis of rat muscle fibers
    • Danieli Betto, D., Zerbato, E. and Betto, R. 1986. Type I, 2A and 2B myosin heavy chain electrophoretic analysis of rat muscle fibers. Biochem. Biophys. Res. Commun. 138: 981-987.
    • (1986) Biochem. Biophys. Res. Commun. , vol.138 , pp. 981-987
    • Danieli Betto, D.1    Zerbato, E.2    Betto, R.3
  • 12
    • 0017158009 scopus 로고
    • Light chains of carp and pike skeletal muscle myosins. Isolation and characterization of the most anodic light chain on alkaline pH electrophoresis
    • Focant, B. and Huriaux, F. 1976. Light chains of carp and pike skeletal muscle myosins. Isolation and characterization of the most anodic light chain on alkaline pH electrophoresis. FEBS Lett. 65: 16-19.
    • (1976) FEBS Lett. , vol.65 , pp. 16-19
    • Focant, B.1    Huriaux, F.2
  • 13
    • 0017080215 scopus 로고
    • Subunit composition offish myofibrils: The light chains of myosin
    • Focant, B. Huriaux, F. and Johnston, I.A. 1976. Subunit composition offish myofibrils: the light chains of myosin. Int. J. Biochem. 7: 129-133.
    • (1976) Int. J. Biochem. , vol.7 , pp. 129-133
    • Focant, B.1    Huriaux, F.2    Johnston, I.A.3
  • 14
    • 0000623058 scopus 로고
    • Myosin, parvalbumin and myofibril expression in barbel (Barbus barbus L.) lateral white muscle during development
    • Focant, B., Huriaux, F., Vandewalle, P., Castelli, M. and Goessens, G. 1992. Myosin, parvalbumin and myofibril expression in barbel (Barbus barbus L.) lateral white muscle during development. Fish Physiol. Biochem. 10: 133-143.
    • (1992) Fish Physiol. Biochem. , vol.10 , pp. 133-143
    • Focant, B.1    Huriaux, F.2    Vandewalle, P.3    Castelli, M.4    Goessens, G.5
  • 16
  • 17
    • 0033119870 scopus 로고    scopus 로고
    • Muscle parvalbumin isoforms of Clarias gariepinus, Heterobranchus longifilis and Chrysichthys auratus: Isolation, characterization, and expression during development
    • Focant, B., Mélot, F., Collin, S., Chikou, A., Vandewalle, P. and Huriaux, F. 1999. Muscle parvalbumin isoforms of Clarias gariepinus, Heterobranchus longifilis and Chrysichthys auratus: isolation, characterization, and expression during development. J. Fish Biol. 54: 832-851.
    • (1999) J. Fish Biol. , vol.54 , pp. 832-851
    • Focant, B.1    Mélot, F.2    Collin, S.3    Chikou, A.4    Vandewalle, P.5    Huriaux, F.6
  • 18
    • 0002726776 scopus 로고
    • Calcium movements between myofibrils, parvalbumins and sarcoplasmic reticulum in muscle
    • Edited by R.H. Wasserman, R.A. Corradino, E. Carafoli, R.H. Kretsinger, D.H. MacLennan and F.L. Siegel. Elsevier, Amsterdam, North-Holland
    • Gillis, J.M. and Gerday, Ch. 1977. Calcium movements between myofibrils, parvalbumins and sarcoplasmic reticulum in muscle. In: Calcium-binding Proteins and Calcium Function. pp. 193-196. Edited by R.H. Wasserman, R.A. Corradino, E. Carafoli, R.H. Kretsinger, D.H. MacLennan and F.L. Siegel. Elsevier, Amsterdam, North-Holland.
    • (1977) Calcium-binding Proteins and Calcium Function , pp. 193-196
    • Gillis, J.M.1    Gerday, Ch.2
  • 19
    • 84996139831 scopus 로고    scopus 로고
    • Perspectives on clariid culture in Africa
    • The Biology and Culture of Catfishes. Edited by M. Legendre and J.-P. Proteau
    • Hecht, T., Oellermann, L. and Verheust, L. 1996. Perspectives on clariid culture in Africa. In: The Biology and Culture of Catfishes. Edited by M. Legendre and J.-P. Proteau. Aquat. Living Resour. 9 Special Issue: 197-206.
    • (1996) Aquat. Living Resour. , vol.9 , Issue.SPEC. ISSUE , pp. 197-206
    • Hecht, T.1    Oellermann, L.2    Verheust, L.3
  • 20
    • 0028269716 scopus 로고
    • Isolation and characterization of tropomyosin from fish muscle
    • Heeley, D.H. and Hong, C. 1994. Isolation and characterization of tropomyosin from fish muscle. Comp. Biochem. Physiol. 108B: 95-106.
    • (1994) Comp. Biochem. Physiol. , vol.108 B , pp. 95-106
    • Heeley, D.H.1    Hong, C.2
  • 22
    • 0017593105 scopus 로고
    • Isolation and characterization of the three light chains from carp white muscle myosin
    • Huriaux, F. and Focant, B. 1977. Isolation and characterization of the three light chains from carp white muscle myosin. Arch. Int. Physiol. Biochim. 85: 917-929.
    • (1977) Arch. Int. Physiol. Biochim. , vol.85 , pp. 917-929
    • Huriaux, F.1    Focant, B.2
  • 23
    • 0022295295 scopus 로고
    • Electrophoretic and immunological study of myosin light chains from freshwater teleost fishes
    • Huriaux, F. and Focant, B. 1985. Electrophoretic and immunological study of myosin light chains from freshwater teleost fishes. Comp. Biochem. Physiol. 82B: 737-743.
    • (1985) Comp. Biochem. Physiol. , vol.82 B , pp. 737-743
    • Huriaux, F.1    Focant, B.2
  • 24
    • 0025259979 scopus 로고
    • Electrophoretic comparison of myosin light chains and parvalbumins of trunk and head muscles from two barbel (Barbus barbus) populations
    • Huriaux, F. Vandewalle, P., Philippart, J.C. and Focant, B. 1990. Electrophoretic comparison of myosin light chains and parvalbumins of trunk and head muscles from two barbel (Barbus barbus) populations. Comp. Biochem. Physiol. 97B: 547-553.
    • (1990) Comp. Biochem. Physiol. , vol.97 B , pp. 547-553
    • Huriaux, F.1    Vandewalle, P.2    Philippart, J.C.3    Focant, B.4
  • 25
    • 0026093788 scopus 로고
    • Myosin heavy chain isoforms in white, red and ventricle muscles of barbel (Barbus barbus L.)
    • Huriaux, F., Vandewalle, P. and Focant, B. 1991. Myosin heavy chain isoforms in white, red and ventricle muscles of barbel (Barbus barbus L.). Comp. Biochem. Physiol. 100B: 309-312.
    • (1991) Comp. Biochem. Physiol. , vol.100 B , pp. 309-312
    • Huriaux, F.1    Vandewalle, P.2    Focant, B.3
  • 26
    • 0029915173 scopus 로고    scopus 로고
    • Parvalbumin isotypes in white muscle from three teleost fish: Characterization and their expression during development
    • Huriaux, F., Mélot, F., Vandewalle, P., Collin, S. and Focant, B. 1996. Parvalbumin isotypes in white muscle from three teleost fish: characterization and their expression during development. Comp. Biochem. Physiol. 113B: 475-484.
    • (1996) Comp. Biochem. Physiol. , vol.113 B , pp. 475-484
    • Huriaux, F.1    Mélot, F.2    Vandewalle, P.3    Collin, S.4    Focant, B.5
  • 27
    • 0031128292 scopus 로고    scopus 로고
    • Characterization of parvalbumin isotypes in white muscle from the barbel and expression during development
    • Huriaux, F., Collin, S., Vandewalle, P., Philippart, J.C. and Focant, B. 1997. Characterization of parvalbumin isotypes in white muscle from the barbel and expression during development. J. Fish Biol. 50: 821-836.
    • (1997) J. Fish Biol. , vol.50 , pp. 821-836
    • Huriaux, F.1    Collin, S.2    Vandewalle, P.3    Philippart, J.C.4    Focant, B.5
  • 28
    • 0031924001 scopus 로고    scopus 로고
    • Scaling of intrinsic contractile properties and myofibrillar protein composition of fast muscle in the fish Myoxocephalus scorpius L
    • James, R.S., Cole, N.J., Davies, M.L.F. and Johnston, I.A. 1998. Scaling of intrinsic contractile properties and myofibrillar protein composition of fast muscle in the fish Myoxocephalus scorpius L. J. Exp. Biol. 201: 901-912.
    • (1998) J. Exp. Biol. , vol.201 , pp. 901-912
    • James, R.S.1    Cole, N.J.2    Davies, M.L.F.3    Johnston, I.A.4
  • 30
    • 0030950503 scopus 로고    scopus 로고
    • Temperature and developmental plasticity of muscle phenotype in herring larvae
    • Johnston, I.A., Cole, N.J., Viera, V.L.A. and Davidson, I. 1997. Temperature and developmental plasticity of muscle phenotype in herring larvae. J. Exp. Biol. 200: 849-868.
    • (1997) J. Exp. Biol. , vol.200 , pp. 849-868
    • Johnston, I.A.1    Cole, N.J.2    Viera, V.L.A.3    Davidson, I.4
  • 31
    • 0027515444 scopus 로고
    • Diversity of native myosin and myosin heavy chain in fish skeletal muscles
    • Karasinski, J. 1993. Diversity of native myosin and myosin heavy chain in fish skeletal muscles. Comp. Biochem. Physiol. 106B: 1041-1047.
    • (1993) Comp. Biochem. Physiol. , vol.106 B , pp. 1041-1047
    • Karasinski, J.1
  • 32
    • 0039640978 scopus 로고
    • Polymorphism of myosin isoenzymes and myosin heavy chains in histochemically typed skeletal muscles of the roach (Rutilus rutilus L., Cyprinidae, Fish)
    • Karasinski, J. and Kilarski, W. 1989. Polymorphism of myosin isoenzymes and myosin heavy chains in histochemically typed skeletal muscles of the roach (Rutilus rutilus L., Cyprinidae, Fish). Comp. Biochem. Physiol. 92B: 727-731.
    • (1989) Comp. Biochem. Physiol. , vol.92 B , pp. 727-731
    • Karasinski, J.1    Kilarski, W.2
  • 33
    • 0028950477 scopus 로고
    • Myogenic cells in development and growth of fish
    • Koumans, J.T.M. and Akster, H.A. 1995. Myogenic cells in development and growth of fish. Comp. Biochem. Physiol. 110A: 3-20.
    • (1995) Comp. Biochem. Physiol. , vol.110 A , pp. 3-20
    • Koumans, J.T.M.1    Akster, H.A.2
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Lond.
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, Lond. 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 84988989288 scopus 로고
    • Développement et tolérance à la température des œufs de Heterobranchus longifilis, et comparaison des développements larvaires de H.longifilis et de Clarias gariepinus (Teleostei, Clariidae)
    • Legendre, M. and Teugels, G.G. 1991. Développement et tolérance à la température des œufs de Heterobranchus longifilis, et comparaison des développements larvaires de H.longifilis et de Clarias gariepinus (Teleostei, Clariidae). Aquat. Living Resour. 4: 227-240.
    • (1991) Aquat. Living Resour. , vol.4 , pp. 227-240
    • Legendre, M.1    Teugels, G.G.2
  • 36
    • 0001893548 scopus 로고
    • A comparative study on morphology, growth rate and reproduction of Clarias gariepinus (Burchell, 1822), Heterobranchus longifilis Valenciennes, 1840, and their reciprocal hybrids (Pisces, Clariidae)
    • Legendre, M., Teugels, G.G., Cauty, C. and Jalabert, B. 1992. A comparative study on morphology, growth rate and reproduction of Clarias gariepinus (Burchell, 1822), Heterobranchus longifilis Valenciennes, 1840, and their reciprocal hybrids (Pisces, Clariidae). J. Fish Biol. 40: 59-79.
    • (1992) J. Fish Biol. , vol.40 , pp. 59-79
    • Legendre, M.1    Teugels, G.G.2    Cauty, C.3    Jalabert, B.4
  • 37
    • 0025636026 scopus 로고
    • Myosin isoforms in red and white muscles of some marine teleost fishes
    • Martinez, I. Ofstad, R. and Olsen, R.L. 1990. Myosin isoforms in red and white muscles of some marine teleost fishes. J. Muscle Res. Cell Motil. 11: 489-495.
    • (1990) J. Muscle Res. Cell Motil. , vol.11 , pp. 489-495
    • Martinez, I.1    Ofstad, R.2    Olsen, R.L.3
  • 38
    • 0025969515 scopus 로고
    • Comparison of myosin isoenzymes present in skeletal and cardiac muscles of the Arctic charr Salvelinus alpinus (L.). Sequential expression of different myosin heavy chains during development of the fast white skeletal muscle
    • Martinez, I. Christiansen, J.S., Ofstad, R. and Olsen, R.L. 1991. Comparison of myosin isoenzymes present in skeletal and cardiac muscles of the Arctic charr Salvelinus alpinus (L.). Sequential expression of different myosin heavy chains during development of the fast white skeletal muscle. Eur. J. Biochem. 195: 743-753.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 743-753
    • Martinez, I.1    Christiansen, J.S.2    Ofstad, R.3    Olsen, R.L.4
  • 39
    • 0027496841 scopus 로고
    • Myofibrillar proteins in skeletal muscles of parr, smolt and adult Atlantic salmon (Salmo salar L.). Comparison with another salmonid, the Arctic charr Salvelinus alpinus (L.)
    • Martinez, I., Bang, B., Hatlen, B. and Blix, P. 1993. Myofibrillar proteins in skeletal muscles of parr, smolt and adult Atlantic salmon (Salmo salar L.). Comparison with another salmonid, the Arctic charr Salvelinus alpinus (L.). Comp. Biochem. Physiol. 106B: 1021-1028.
    • (1993) Comp. Biochem. Physiol. , vol.106 B , pp. 1021-1028
    • Martinez, I.1    Bang, B.2    Hatlen, B.3    Blix, P.4
  • 40
    • 0028013468 scopus 로고
    • Myofibrillar proteins in developing white muscle of the Arctic charr, Salvelinus alpinus (L.)
    • Martinez, I. and Christiansen, J.S. 1994. Myofibrillar proteins in developing white muscle of the Arctic charr, Salvelinus alpinus (L.) Comp. Biochem. Physiol. 107B: 11-20.
    • (1994) Comp. Biochem. Physiol. , vol.107 B , pp. 11-20
    • Martinez, I.1    Christiansen, J.S.2
  • 41
    • 0020478366 scopus 로고
    • Purification and characterization of troponin C from pike muscle: A comparative spectroscopic study with rabbit skeletal muscle troponin C
    • McCubbin, W.D., Oikawa, K., Sykes, B.D. and Kay, C.M. 1982. Purification and characterization of troponin C from pike muscle: a comparative spectroscopic study with rabbit skeletal muscle troponin C. Biochemistry 21: 5948-5956.
    • (1982) Biochemistry , vol.21 , pp. 5948-5956
    • McCubbin, W.D.1    Oikawa, K.2    Sykes, B.D.3    Kay, C.M.4
  • 42
    • 0019919233 scopus 로고
    • Physiological effects accompanying the removal of myosin LC2 from skinned skeletal muscle fibers
    • Moss, R.L., Giulian, G.G. and Greaser, M.L. 1982. Physiological effects accompanying the removal of myosin LC2 from skinned skeletal muscle fibers. J. Biol. Chem. 257: 8588-8591.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8588-8591
    • Moss, R.L.1    Giulian, G.G.2    Greaser, M.L.3
  • 43
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.H. 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250: 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 44
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell, P.Z., Goodman, H.M. and O'Farrell, P.H. 1977. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12: 1133-1141.
    • (1977) Cell , vol.12 , pp. 1133-1141
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 45
    • 84996128270 scopus 로고    scopus 로고
    • Nouvelles espèces de poissons-chats pour le développement de la pisciculture africaine
    • The Biology and Culture of Catfishes. Edited by M. Legendre and J.-P. Proteau
    • Otémé, Z., Hem, J.S. and Legendre, M. 1996. Nouvelles espèces de poissons-chats pour le développement de la pisciculture africaine. In: The Biology and Culture of Catfishes. Edited by M. Legendre and J.-P. Proteau. Aquat. Living Resour. 9 Special Issue: 207-217.
    • (1996) Aquat. Living Resour. , vol.9 , Issue.SPEC. ISSUE , pp. 207-217
    • Otémé, Z.1    Hem, J.S.2    Legendre, M.3
  • 46
    • 0025653451 scopus 로고
    • Cellular and molecular diversities of mammalian skeletal muscle fibers
    • Pette, D. and Staron, R.S. 1990. Cellular and molecular diversities of mammalian skeletal muscle fibers. Rev. Physiol. Biochem. Pharmacol. 116: 1-76.
    • (1990) Rev. Physiol. Biochem. Pharmacol. , vol.116 , pp. 1-76
    • Pette, D.1    Staron, R.S.2
  • 47
    • 0016258106 scopus 로고
    • Myosin light-chain kinase, a new enzyme from striated muscle
    • Pires, E., Perry, S.V. and Thomas, M.A.W. 1974. Myosin light-chain kinase, a new enzyme from striated muscle. FEBS Lett. 41: 292-296.
    • (1974) FEBS Lett. , vol.41 , pp. 292-296
    • Pires, E.1    Perry, S.V.2    Thomas, M.A.W.3
  • 48
    • 0022345897 scopus 로고
    • Comparative study of myosins present in the lateral muscle of some fish: Species variations in myosin isoforms and their distribution in red, pink and white muscle
    • Rowlerson, A., Scapolo, P.A., Mascarello, F., Carpenè, E. and Veggetti, A. 1985. Comparative study of myosins present in the lateral muscle of some fish: species variations in myosin isoforms and their distribution in red, pink and white muscle. J. Muscle Res. Cell Motil. 6: 601-640.
    • (1985) J. Muscle Res. Cell Motil. , vol.6 , pp. 601-640
    • Rowlerson, A.1    Scapolo, P.A.2    Mascarello, F.3    Carpenè, E.4    Veggetti, A.5
  • 49
    • 0023741330 scopus 로고
    • Developmental transitions of myosin isoforms and organisation of the lateral muscle in the teleost Dicentrarchus labrax (L.)
    • Scapolo, P.A., Veggetti, A., Mascarello, F. and Romanello, M.G. 1988. Developmental transitions of myosin isoforms and organisation of the lateral muscle in the teleost Dicentrarchus labrax (L.). Anat. Embryol. 178: 287-295.
    • (1988) Anat. Embryol. , vol.178 , pp. 287-295
    • Scapolo, P.A.1    Veggetti, A.2    Mascarello, F.3    Romanello, M.G.4
  • 50
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: Gene regulation and functional significance
    • Schiaffino, S. and Reggiani, C. 1996. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol. Rev. 76: 371-423.
    • (1996) Physiol. Rev. , vol.76 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 51
    • 0020587107 scopus 로고
    • Analysis of differences between Coomassie blue stain and silver stain procedures in polyacrylamide gels: Conditions for the detection of calmodulin and troponin C
    • Schleicher, M. and Watterson, D.M. 1983. Analysis of differences between Coomassie blue stain and silver stain procedures in polyacrylamide gels: conditions for the detection of calmodulin and troponin C. Anal. Biochem. 131: 312-317.
    • (1983) Anal. Biochem. , vol.131 , pp. 312-317
    • Schleicher, M.1    Watterson, D.M.2
  • 52
    • 0011605584 scopus 로고
    • Muscle fibrils: Solubilization and gel electrophoresis
    • Sender, P.M. 1971. Muscle fibrils: solubilization and gel electrophoresis. FEBS Lett. 17: 106-110.
    • (1971) FEBS Lett. , vol.17 , pp. 106-110
    • Sender, P.M.1
  • 53
    • 0015980244 scopus 로고
    • A new method of preparation of troponin I (inhibitory protein) using affinity chromatography. Evidence for three different forms of troponin I in striated muscle
    • Syska, H., Perry, S.V. and Trayer, I.P. 1974. A new method of preparation of troponin I (inhibitory protein) using affinity chromatography. Evidence for three different forms of troponin I in striated muscle. FEBS Lett. 40: 253-257.
    • (1974) FEBS Lett. , vol.40 , pp. 253-257
    • Syska, H.1    Perry, S.V.2    Trayer, I.P.3
  • 54
    • 0021659767 scopus 로고
    • Chordate muscle actins differ distinctly from invertebrate muscle actins. The evolution of the different vertebrate muscle actins
    • Vandekerckhove, J. and Weber, K. 1984. Chordate muscle actins differ distinctly from invertebrate muscle actins. The evolution of the different vertebrate muscle actins. J. Mol. Biol. 179: 391-413.
    • (1984) J. Mol. Biol. , vol.179 , pp. 391-413
    • Vandekerckhove, J.1    Weber, K.2
  • 55
    • 0031080125 scopus 로고    scopus 로고
    • Postembryonic development of the cephalic region in Heterobranchus longifilis
    • Vandewalle, P., Gluckmann, I., Baras, E., Huriaux, F. and Focant, B. 1997. Postembryonic development of the cephalic region in Heterobranchus longifilis. J. Fish Biol. 50: 227-253.
    • (1997) J. Fish Biol. , vol.50 , pp. 227-253
    • Vandewalle, P.1    Gluckmann, I.2    Baras, E.3    Huriaux, F.4    Focant, B.5
  • 56
    • 0001214914 scopus 로고
    • Dynamics of increase in muscle fibers in fishes in relation to size and growth
    • Weatherley, A.H. and Gill, H.S. 1985. Dynamics of increase in muscle fibers in fishes in relation to size and growth. Experientia 41: 353-354.
    • (1985) Experientia , vol.41 , pp. 353-354
    • Weatherley, A.H.1    Gill, H.S.2
  • 57
    • 0020050780 scopus 로고
    • Effect of electrical stimulation and exercise on the phosphorylation state of myosin light chains from fish skeletal muscle
    • Yancey, P.H. and Johnston, I.A. 1982. Effect of electrical stimulation and exercise on the phosphorylation state of myosin light chains from fish skeletal muscle. Pflügers Arch. 393: 334-339.
    • (1982) Pflügers Arch. , vol.393 , pp. 334-339
    • Yancey, P.H.1    Johnston, I.A.2


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