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Volumn 30, Issue 3-4, 2009, Pages 125-137

Different fibre populations distinguished by their calcium transient characteristics in enzymatically dissociated murine flexor digitorum brevis and soleus muscles

Author keywords

Calcium transients; Fibre types; Flexor digitorum brevis; Myosin adenosine triphosphatase activity; Soleus

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CALCIUM ION; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; MYOSIN; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 69549105810     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-009-9181-1     Document Type: Article
Times cited : (31)

References (58)
  • 1
    • 0005458810 scopus 로고
    • Metabolic changes in muscle during exercise: Their effects on muscle function
    • D Allen S Duty H Westerblad 1993 Metabolic changes in muscle during exercise: their effects on muscle function Proc Aust Physiol Pharmacol Soc 24 65 75
    • (1993) Proc Aust Physiol Pharmacol Soc , vol.24 , pp. 65-75
    • Allen, D.1    Duty, S.2    Westerblad, H.3
  • 2
    • 0024458592 scopus 로고
    • Maximal shortening velocities, isomyosins and fibre types in soleus muscle of mice, rats and guinea pigs
    • G Asmussen G Maréchal 1989 Maximal shortening velocities, isomyosins and fibre types in soleus muscle of mice, rats and guinea pigs J Physiol 416 245 254
    • (1989) J Physiol , vol.416 , pp. 245-254
    • Asmussen, G.1    Maréchal, G.2
  • 3
    • 0023820311 scopus 로고
    • Three fast myosin heavy chains in adult rat skeletal muscle
    • A Bär D Pette 1988 Three fast myosin heavy chains in adult rat skeletal muscle FEBS Lett 235 1, 2 153 155
    • (1988) FEBS Lett , vol.235 , Issue.1-2 , pp. 153-155
    • Bär, A.1    Pette, D.2
  • 4
    • 0015011589 scopus 로고
    • Histochemical, biochemical, and contractile properties of red, white, and intermediate fibers
    • R Barnard V Edgerton T Furukawa J Peter 1971 Histochemical, biochemical, and contractile properties of red, white, and intermediate fibers Am J Physiol 220 410 414
    • (1971) Am J Physiol , vol.220 , pp. 410-414
    • Barnard, R.1    Edgerton, V.2    Furukawa, T.3    Peter, J.4
  • 5
    • 0041353449 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum calcium release compared in slow-twitch and fast-twitch fibres of mouse muscle
    • DOI 10.1113/jphysiol.2003.041608
    • S Baylor S Hollingworth 2003 Sarcoplasmic reticulum calcium release compared in slow-twitch and fast-twitch fibres of mouse muscle J Physiol 551 125 138 10.1113/jphysiol.2003.041608 (Pubitemid 37062917)
    • (2003) Journal of Physiology , vol.551 , Issue.1 , pp. 125-138
    • Baylor, S.M.1    Hollingworth, S.2
  • 6
    • 0017666492 scopus 로고
    • Physiological properties of dissociated muscle fibres obtained from innervated and denervated adult rat muscle
    • A Bekoff W Betz 1977 Physiological properties of dissociated muscle fibres obtained from innervated and denervated adult rat muscle J Physiol 271 25 40
    • (1977) J Physiol , vol.271 , pp. 25-40
    • Bekoff, A.1    Betz, W.2
  • 7
    • 0030068816 scopus 로고    scopus 로고
    • Enhanced electrophoretic separation and resolution of myosin heavy chains in mammalian and avian skeletal muscles
    • DOI 10.1006/abio.1996.0003
    • E Blough E Rennie F Zhang P Reiser 1996 Enhanced electrophoretic separation and resolution of myosin heavy chains in mammalian and avian skeletal muscles Anal Biochem 233 31 35 10.1006/abio.1996.0003 (Pubitemid 26036361)
    • (1996) Analytical Biochemistry , vol.233 , Issue.1 , pp. 31-35
    • Blough, E.R.1    Rennie, E.R.2    Zhang, F.3    Reiser, P.J.4
  • 9
    • 0033823157 scopus 로고    scopus 로고
    • Human skeletal muscle fibres: Molecular and functional diversity
    • DOI 10.1016/S0079-6107(00)00006-7, PII S0079610700000067
    • R Bottinelli C Reggiani 2000 Human skeletal muscle fibres: molecular and functional diversity Prog Biophys Mol Biol 73 195 262 10.1016/S0079-6107(00) 00006-7 (Pubitemid 30695145)
    • (2000) Progress in Biophysics and Molecular Biology , vol.73 , Issue.2-4 , pp. 195-262
    • Bottinelli, R.1    Reggiani, C.2
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3
    • M Bradford 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding Anal Biochem 72 248 254 10.1016/0003-2697(76)90527-3
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 11
    • 0014530017 scopus 로고
    • Some comments on the hitochemical characterization of muscle adenosine triphosphatase
    • M Brooke K Kaiser 1969 Some comments on the hitochemical characterization of muscle adenosine triphosphatase J Histochem Cytochem 17 431 432
    • (1969) J Histochem Cytochem , vol.17 , pp. 431-432
    • Brooke, M.1    Kaiser, K.2
  • 12
    • 0014838245 scopus 로고
    • Three "myosin adenosine triphosphatase" systems: The nature of their pH lability and sulfhydryl dependence
    • M Brooke K Kaiser 1970 Three "myosin adenosine triphosphatase" systems: the nature of their pH lability and sulfhydryl dependence J Histochem Cytochem 18 9 670 672
    • (1970) J Histochem Cytochem , vol.18 , Issue.9 , pp. 670-672
    • Brooke, M.1    Kaiser, K.2
  • 13
    • 0015156701 scopus 로고
    • Mammalian motor units: Physiological-histochemical correlation in three types in cat gastrocnemius
    • 10.1126/science.174.4010.709
    • R Burke D Levine F Zajac 1971 Mammalian motor units: physiological- histochemical correlation in three types in cat gastrocnemius Science 174 709 712 10.1126/science.174.4010.709
    • (1971) Science , vol.174 , pp. 709-712
    • Burke, R.1    Levine, D.2    Zajac, F.3
  • 14
    • 69549106654 scopus 로고    scopus 로고
    • Functional identification of fiber types in enzymatically dissociated murine flexor digitorum brevis and soleus muscles
    • J Calderón-Vélez P Bolaños C Caputo 2009 Functional identification of fiber types in enzymatically dissociated murine flexor digitorum brevis and soleus muscles Biophys J 96 3-S1 233a
    • (2009) Biophys J , vol.96 , Issue.3 S1
    • Calderón-Vélez, J.1    Bolaños, P.2    Caputo, C.3
  • 15
    • 17844381619 scopus 로고    scopus 로고
    • Calcium transients in developing mouse skeletal muscle fibres
    • DOI 10.1113/jphysiol.2004.081034
    • J Capote P Bolaños R Schuhmeier C Caputo 2005 Calcium transients in developing mouse skeletal muscle fibres J Physiol 564 2 451 464 10.1113/jphysiol.2004.081034 (Pubitemid 40585045)
    • (2005) Journal of Physiology , vol.564 , Issue.2 , pp. 451-464
    • Capote, J.1    Bolanos, P.2    Schuhmeier, R.P.3    Melzer, W.4    Caputo, C.5
  • 16
    • 0028819073 scopus 로고
    • Calcium transients in intact rat skeletal muscle fibers in agarosa gel
    • S Carroll M Klein M Schneider 1995 Calcium transients in intact rat skeletal muscle fibers in agarosa gel Am J Physiol 269 C28 C34
    • (1995) Am J Physiol , vol.269
    • Carroll, S.1    Klein, M.2    Schneider, M.3
  • 17
    • 0030811886 scopus 로고    scopus 로고
    • Decay of calcium transients after electrical stimulation in rat fast- and slow-twitch skeletal muscle fibres
    • DOI 10.1111/j.1469-7793.1997.573bm.x
    • S Carroll M Klein M Schneider 1997 Decay of calcium transients after electrical stimulation in rat fast- and slow-twitch skeletal muscle fibres J Physiol 501 3 573 588 10.1111/j.1469-7793.1997.573bm.x (Pubitemid 27300012)
    • (1997) Journal of Physiology , vol.501 , Issue.3 , pp. 573-588
    • Carroll, S.L.1    Klein, M.G.2    Schneider, M.F.3
  • 18
    • 0020328821 scopus 로고
    • Calcium-binding protein parvalbumin is associated with fast contracting muscle fibres
    • 10.1038/297504a0
    • M Celio C Heizmann 1982 Calcium-binding protein parvalbumin is associated with fast contracting muscle fibres Nature 297 504 506 10.1038/297504a0
    • (1982) Nature , vol.297 , pp. 504-506
    • Celio, M.1    Heizmann, C.2
  • 20
    • 0015257535 scopus 로고
    • Dynamic properties of mammalian skeletal muscles
    • R Close 1972 Dynamic properties of mammalian skeletal muscles Physiol Rev 52 1 129 197
    • (1972) Physiol Rev , vol.52 , Issue.1 , pp. 129-197
    • Close, R.1
  • 21
    • 0030024488 scopus 로고    scopus 로고
    • Composition and size of type I, IIA, IID/X, and IIB fibers and citrate synthase activity of rat muscle
    • M Delp C Duan 1996 Composition and size of type I, IIA, IID/X, and IIB fibers and citrate synthase activity of rat muscle J Appl Physiol 80 1 261 270
    • (1996) J Appl Physiol , vol.80 , Issue.1 , pp. 261-270
    • Delp, M.1    Duan, C.2
  • 22
    • 0036190982 scopus 로고    scopus 로고
    • Characterization of the calcium release domains during excitation-contraction coupling in skeletal muscle fibres
    • DOI 10.1007/s004240100719
    • M DiFranco D Novo JL Vergara 2002 Characterization of the calcium release domains during excitation-contraction coupling in skeletal muscle fibers Pflugers Arch 443 508 519 10.1007/s004240100719 (Pubitemid 34185055)
    • (2002) Pflugers Archiv European Journal of Physiology , vol.443 , Issue.4 , pp. 508-519
    • DiFranco, M.1    Novo, D.2    Vergara, J.L.3
  • 23
    • 69549087181 scopus 로고
    • 2 Bailliere Tindall London
    • Dubowitz V (1985) Muscle biopsy: a practical approach, 2nd edn. Bailliere Tindall, London
    • (1985)
    • Dubowitz, V.1
  • 24
    • 0001873039 scopus 로고
    • A comparative histochemical study of oxidative enzyme and phophorylase activity in skeletal muscle
    • 10.1007/BF00744575
    • V Dubowitz A Pearse 1960 A comparative histochemical study of oxidative enzyme and phophorylase activity in skeletal muscle Histochemie 2 105 117 10.1007/BF00744575
    • (1960) Histochemie , vol.2 , pp. 105-117
    • Dubowitz, V.1    Pearse, A.2
  • 25
    • 0023492149 scopus 로고
    • Distribution of calcium ATPase in the sarcoplasmic reticulum of fast- and slow-twitch muscles determined with monoclonal antibodies
    • 10.1007/BF01871228
    • A Dulhunty M Banyard C Medveczky 1987 Distribution of calcium ATPase in the sarcoplasmic reticulum of fast- and slow-twitch muscles determined with monoclonal antibodies J Membr Biol 99 79 92 10.1007/BF01871228
    • (1987) J Membr Biol , vol.99 , pp. 79-92
    • Dulhunty, A.1    Banyard, M.2    Medveczky, C.3
  • 26
    • 0024320228 scopus 로고
    • Parvalbumin in mouse muscle in vivo and in vitro
    • DOI 10.1111/j.1432-0436.1989.tb00808.x
    • M Ecob-Prince E Leberer 1989 Parvalbumin in mouse muscle in vivo and in vitro Differentiation 40 10 16 10.1111/j.1432-0436.1989.tb00808.x (Pubitemid 19149288)
    • (1989) Differentiation , vol.40 , Issue.1 , pp. 10-16
    • Ecob-Prince, M.S.1    Leberer, E.2
  • 27
    • 0000504097 scopus 로고
    • The essentiality of histo- and cytochemical studies of skeletal muscle in the investigation of neuromuscular disease
    • W Engel 1962 The essentiality of histo- and cytochemical studies of skeletal muscle in the investigation of neuromuscular disease Neurology 12 778 794
    • (1962) Neurology , vol.12 , pp. 778-794
    • Engel, W.1
  • 28
    • 0018819391 scopus 로고
    • Calcium transients in mammalian muscles
    • 10.1038/284560a0
    • F Eusebi R Miledi T Takahashi 1980 Calcium transients in mammalian muscles Nature 284 560 561 10.1038/284560a0
    • (1980) Nature , vol.284 , pp. 560-561
    • Eusebi, F.1    Miledi, R.2    Takahashi, T.3
  • 29
    • 0023821115 scopus 로고
    • The Ca2+ ATPase content of slow and fast twitch fibers of guinea pig
    • 10.1002/mus.880110607
    • D Ferguson C Franzini-Armstrong 1988 The Ca2+ ATPase content of slow and fast twitch fibers of guinea pig Muscle Nerve 11 561 570 10.1002/mus.880110607
    • (1988) Muscle Nerve , vol.11 , pp. 561-570
    • Ferguson, D.1    Franzini-Armstrong, C.2
  • 30
    • 0024162292 scopus 로고
    • Discrimination between fast- and slow-twitch fibres of guinea pig skeletal muscle using the relative surface density of junctional transverse tubule membrane
    • DOI 10.1007/BF01774067
    • C Franzini-Armstrong D Ferguson C Champ 1988 Discrimination between fast- and slow-twitch fibres of guinea pig skeletal muscle using the relative surface density of junctional transverse tubule membrane J Muscle Res Cell Motil 9 403 414 10.1007/BF01774067 (Pubitemid 18279366)
    • (1988) Journal of Muscle Research and Cell Motility , vol.9 , Issue.5 , pp. 403-414
    • Franzini-Armstrong, C.1    Ferguson, D.G.2    Champ, C.3
  • 31
    • 0026073770 scopus 로고
    • Direct correlation of parvalbumin levels with myosin isoforms and succinate dehydrogenase activity on frozen sections of rodent muscle
    • E Füchtbauer A Rowlerson K Gotz G Friedrich K Mabuchi J Gergely, et al. 1991 Direct correlation of parvalbumin levels with myosin isoforms and succinate dehydrogenase activity on frozen sections of rodent muscle J Histochem Cytochem 39 3 355 361
    • (1991) J Histochem Cytochem , vol.39 , Issue.3 , pp. 355-361
    • Füchtbauer, E.1    Rowlerson, A.2    Gotz, K.3    Friedrich, G.4    Mabuchi, K.5    Gergely, J.6
  • 32
    • 0020286673 scopus 로고
    • Parvalbumins and muscle relaxation: A computer simulation study
    • 10.1007/BF00712090
    • J Gillis D Thomason J Lefévre R Kretsinger 1982 Parvalbumins and muscle relaxation: a computer simulation study J Muscle Res Cell Motil 3 377 398 10.1007/BF00712090
    • (1982) J Muscle Res Cell Motil , vol.3 , pp. 377-398
    • Gillis, J.1    Thomason, D.2    Lefévre, J.3    Kretsinger, R.4
  • 33
    • 18244417721 scopus 로고    scopus 로고
    • 2+ in single intact muscle fibres from transgenic mice
    • DOI 10.1113/jphysiol.2003.048165
    • E González M Messi Z Zheng O Delbono 2003 Insulin-like growth factor-1 prevents age-related decrease in specific force and intracellular Ca2+ in single intact muscle fibres from transgenic mouse J Physiol 552 833 844 10.1113/jphysiol.2003.048165 (Pubitemid 37428424)
    • (2003) Journal of Physiology , vol.552 , Issue.3 , pp. 833-844
    • Gonzalez, E.1    Messi, M.L.2    Zheng, Z.3    Delbono, O.4
  • 34
    • 0014575646 scopus 로고
    • Qualitative differences between actomyosin ATPase of slow and fast mammalian muscle
    • 10.1016/0014-4886(69)90077-6
    • L Guth F Samaha 1969 Qualitative differences between actomyosin ATPase of slow and fast mammalian muscle Exp Neurol 25 138 152 10.1016/0014-4886(69) 90077-6
    • (1969) Exp Neurol , vol.25 , pp. 138-152
    • Guth, L.1    Samaha, F.2
  • 35
    • 0028924293 scopus 로고
    • Patterns of myosin isoforms in mammalian skeletal muscle fibres
    • 10.1002/jemt.1070300505
    • N Hämäläinen D Pette 1995 Patterns of myosin isoforms in mammalian skeletal muscle fibres Microsc Res Tech 30 381 389 10.1002/jemt.1070300505
    • (1995) Microsc Res Tech , vol.30 , pp. 381-389
    • Hämäläinen, N.1    Pette, D.2
  • 36
    • 33644808902 scopus 로고    scopus 로고
    • 2+-ATPase of the sarcoplasmic reticulum in skeletal and cardiac muscle
    • 10.1111/j.1749-6632.1998.tb08251.x
    • 2+-ATPase of the sarcoplasmic reticulum in skeletal and cardiac muscle Ann N Y Acad Sci 853 1 8 10.1111/j.1749-6632.1998.tb08251.x
    • (1998) Ann N y Acad Sci , vol.853 , pp. 1-8
    • Hasselbach, W.1
  • 37
    • 0020392253 scopus 로고
    • Correlation of parvalbumin concentration with relaxation speed in mammalian muscle
    • 10.1073/pnas.79.23.7243
    • C Heizmann M Berchtold A Rowlerson 1982 Correlation of parvalbumin concentration with relaxation speed in mammalian muscle Proc Natl Acad Sci USA 79 7243 7247 10.1073/pnas.79.23.7243
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 7243-7247
    • Heizmann, C.1    Berchtold, M.2    Rowlerson, A.3
  • 38
    • 0019731776 scopus 로고
    • A comparative study of charge movement in rat and frog skeletal muscle fibres
    • S Hollingworth M Marshall 1981 A comparative study of charge movement in rat and frog skeletal muscle fibres J Physiol 321 583 602
    • (1981) J Physiol , vol.321 , pp. 583-602
    • Hollingworth, S.1    Marshall, M.2
  • 39
    • 0029923677 scopus 로고    scopus 로고
    • Parvalbumin relaxes frog skeletal muscle when sarcoplasmic reticulum Ca2+-ATPase is inhibited
    • Y Jiang J Johnson J Rall 1996 Parvalbumin relaxes frog skeletal muscle when sarcoplasmic reticulum Ca2+-ATPase is inhibited Am J Physiol 270 C411 C417
    • (1996) Am J Physiol , vol.270
    • Jiang, Y.1    Johnson, J.2    Rall, J.3
  • 40
    • 0023040142 scopus 로고
    • Immunochemical quantification of sarcoplasmic reticulum Ca-ATPase, of calsequestrin and of parvalbumin in rabbit skeletal muscles
    • 10.1111/j.1432-1033.1986.tb09607.x
    • E Leberer D Pette 1986 Immunochemical quantification of sarcoplasmic reticulum Ca-ATPase, of calsequestrin and of parvalbumin in rabbit skeletal muscles Eur J Biochem 156 489 496 10.1111/j.1432-1033.1986.tb09607.x
    • (1986) Eur J Biochem , vol.156 , pp. 489-496
    • Leberer, E.1    Pette, D.2
  • 41
    • 0023821258 scopus 로고
    • 2-sequestration by the sarcoplasmic reticulum of fast and slow muscles in normal and dystrophic mice
    • DOI 10.1111/j.1432-1033.1988.tb14090.x
    • E Leberer K Härtner D Pette 1988 Postnatal development of Ca2+-sequestration by the sarcoplasmic reticulum of fast and slow muscles in normal and dystrophic mice Eur J Biochem 174 247 253 10.1111/j.1432-1033.1988. tb14090.x (Pubitemid 18153214)
    • (1988) European Journal of Biochemistry , vol.174 , Issue.2 , pp. 247-253
    • Leberer, E.1    Hartner, K.-T.2    Pette, D.3
  • 42
    • 0027327111 scopus 로고
    • Force-velocity relation and isomyosins in soleus muscles from two strains of mice (C57 and NMRI)
    • 10.1007/BF00374911
    • G Maréchal G Beckers-Bleukx 1993 Force-velocity relation and isomyosins in soleus muscles from two strains of mice (C57 and NMRI) Pflugers Arch 424 478 487 10.1007/BF00374911
    • (1993) Pflugers Arch , vol.424 , pp. 478-487
    • Maréchal, G.1    Beckers-Bleukx, G.2
  • 43
    • 0003062842 scopus 로고
    • Mitochondrial localization of oxidative enzymes: Staining results with two tetrazolium salts
    • A Novikoff S Woo-yung J Drucker 1961 Mitochondrial localization of oxidative enzymes: staining results with two tetrazolium salts J Biophys Biochem Cytol 9 47 61
    • (1961) J Biophys Biochem Cytol , vol.9 , pp. 47-61
    • Novikoff, A.1    Woo-Yung, S.2    Drucker, J.3
  • 44
    • 0000209971 scopus 로고
    • Factors affecting the activity of adenosine triphospahatase and other phosphatases as measured by histochemical techniques
    • H Padykula E Herman 1955 Factors affecting the activity of adenosine triphospahatase and other phosphatases as measured by histochemical techniques J Histochem Cytochem 3 161 170
    • (1955) J Histochem Cytochem , vol.3 , pp. 161-170
    • Padykula, H.1    Herman, E.2
  • 45
    • 77049188994 scopus 로고
    • The specificity of the histochemical method for adenosine triphosphatase
    • H Padykula E Herman 1955 The specificity of the histochemical method for adenosine triphosphatase J Histochem Cytochem 3 170 195
    • (1955) J Histochem Cytochem , vol.3 , pp. 170-195
    • Padykula, H.1    Herman, E.2
  • 46
    • 34047219171 scopus 로고    scopus 로고
    • SERCA pump isoforms: Their role in calcium transport and disease
    • DOI 10.1002/mus.20745
    • M Periasamy A Kalyanasundaram 2007 Serca pump isoforms: their role in calcium transport and disease Muscle Nerve 35 430 442 10.1002/mus.20745 (Pubitemid 46542962)
    • (2007) Muscle and Nerve , vol.35 , Issue.4 , pp. 430-442
    • Periasamy, M.1    Kalyanasundaram, A.2
  • 47
    • 0015493810 scopus 로고
    • Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits
    • 10.1021/bi00764a013
    • J Peter R Barnard V Edgerton C Gillespie K Stempel 1972 Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits Biochemistry 11 14 2627 2633 10.1021/bi00764a013
    • (1972) Biochemistry , vol.11 , Issue.14 , pp. 2627-2633
    • Peter, J.1    Barnard, R.2    Edgerton, V.3    Gillespie, C.4    Stempel, K.5
  • 48
    • 0041883129 scopus 로고
    • Propriétés et structures différentes des muscles rouges et des muscles blancs, chez les Lapins et chez les Raies
    • L Ranvier 1873 Propriétés et structures différentes des muscles rouges et des muscles blancs, chez les Lapins et chez les Raies Compt Rend 77 1030 1034
    • (1873) Compt Rend , vol.77 , pp. 1030-1034
    • Ranvier, L.1
  • 50
  • 52
    • 0026052438 scopus 로고
    • Fiber type-specific distribution of parvalbumin in rabbit skeletal muscle
    • 10.1007/BF00267071
    • T Schmitt D Pette 1991 Fiber type-specific distribution of parvalbumin in rabbit skeletal muscle Histochemistry 96 459 465 10.1007/BF00267071
    • (1991) Histochemistry , vol.96 , pp. 459-465
    • Schmitt, T.1    Pette, D.2
  • 53
    • 0037845309 scopus 로고    scopus 로고
    • Mechanism of inhibition of skeletal muscle actomyosin by N-Benzyl-p-toluenesulfonamide
    • DOI 10.1021/bi026964f
    • M Shaw E Ostap Y Goldman 2003 Mechanism of inhibition of skeletal muscle actomyosin by N-benzyl-p-toluenesulfonamide Biochemistry 42 6128 6135 10.1021/bi026964f (Pubitemid 36605114)
    • (2003) Biochemistry , vol.42 , Issue.20 , pp. 6128-6135
    • Shaw, M.A.1    Ostap, E.M.2    Goldman, Y.E.3
  • 54
    • 0025909566 scopus 로고
    • Correlation between myofibrillar ATPase activity and myosin heavy chain composition in single human muscle fibers
    • 10.1007/BF00266756
    • R Staron 1991 Correlation between myofibrillar ATPase activity and myosin heavy chain composition in single human muscle fibers Histochemistry 96 21 24 10.1007/BF00266756
    • (1991) Histochemistry , vol.96 , pp. 21-24
    • Staron, R.1
  • 55
    • 0000573855 scopus 로고
    • Histochemical classification of individual skeletal muscle fibers of the rat
    • 10.1002/aja.1001100203
    • J Stein H Padykula 1962 Histochemical classification of individual skeletal muscle fibers of the rat Am J Anat 110 103 123 10.1002/aja.1001100203
    • (1962) Am J Anat , vol.110 , pp. 103-123
    • Stein, J.1    Padykula, H.2
  • 56
    • 69549126930 scopus 로고
    • Academic Press New York
    • Szent-Györgyi A (1953) Chemical physiology of contraction in body and heart muscle. Academic Press, New York
    • (1953)
    • Szent-Györgyi, A.1
  • 57
    • 0027452352 scopus 로고
    • Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms
    • R Talmadge R Roy 1993 Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms J Appl Physiol 75 5 2337 2340
    • (1993) J Appl Physiol , vol.75 , Issue.5 , pp. 2337-2340
    • Talmadge, R.1    Roy, R.2
  • 58
    • 72849184174 scopus 로고
    • 10 and menadione on succinic dehydrogenase activity as measured by tetrazolium salt reduction
    • 10 and menadione on succinic dehydrogenase activity as measured by tetrazolium salt reduction J Histochem Cytochem 8 296 303
    • (1960) J Histochem Cytochem , vol.8 , pp. 296-303
    • Watemberg, L.1    Leong, L.2


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