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Volumn 148, Issue 2, 2007, Pages 399-407

Identification of myosin heavy chain isoforms in skeletal muscle of four Southern African wild ruminants

Author keywords

Blesbuck; Game; Human; Kudu; SDS PAGE; Wild ruminants; Wildebeest

Indexed keywords

ISOPROTEIN; MYOSIN ANTIBODY; MYOSIN HEAVY CHAIN; MYOSIN HEAVY CHAIN I; MYOSIN HEAVY CHAIN IIA; MYOSIN HEAVY CHAIN IIX; UNCLASSIFIED DRUG;

EID: 34547565234     PISSN: 10956433     EISSN: 15314332     Source Type: Journal    
DOI: 10.1016/j.cbpa.2007.05.028     Document Type: Article
Times cited : (18)

References (55)
  • 1
    • 30744447897 scopus 로고    scopus 로고
    • New insights into skeletal muscle fibre types in the dog with particular focus towards hybrid myosin phenotypes
    • Acevedo L.M., and Rivero J.L. New insights into skeletal muscle fibre types in the dog with particular focus towards hybrid myosin phenotypes. Cell Tissue Res. 323 (2006) 283-303
    • (2006) Cell Tissue Res. , vol.323 , pp. 283-303
    • Acevedo, L.M.1    Rivero, J.L.2
  • 3
    • 0028352095 scopus 로고
    • Myosin heavy chain isoforms in single fibres from m. vastus lateralis of soccer players: effects of strength-training
    • Andersen J.L., Klitgaard H., Bangsbo J., and Saltin B. Myosin heavy chain isoforms in single fibres from m. vastus lateralis of soccer players: effects of strength-training. Acta Physiol. Scand. 150 (1994) 21-26
    • (1994) Acta Physiol. Scand. , vol.150 , pp. 21-26
    • Andersen, J.L.1    Klitgaard, H.2    Bangsbo, J.3    Saltin, B.4
  • 5
    • 0032915685 scopus 로고    scopus 로고
    • Enhanced protein electrophoresis technique for separating human skeletal-muscle myosin heavy-chain isoforms
    • Bamman M.M., Clarke M.S.F., Talmadge R.J., and Feeback D.L. Enhanced protein electrophoresis technique for separating human skeletal-muscle myosin heavy-chain isoforms. Electrophoresis 20 (1999) 466-468
    • (1999) Electrophoresis , vol.20 , pp. 466-468
    • Bamman, M.M.1    Clarke, M.S.F.2    Talmadge, R.J.3    Feeback, D.L.4
  • 6
    • 0023186436 scopus 로고
    • Exercise training induces transitions of myosin isoform subunits within histochemically typed human muscle fibres
    • Baumann H., Jaggi M., Soland F., Howald H., and Schaub M.C. Exercise training induces transitions of myosin isoform subunits within histochemically typed human muscle fibres. Pflügers Arch. 409 (1987) 349-360
    • (1987) Pflügers Arch. , vol.409 , pp. 349-360
    • Baumann, H.1    Jaggi, M.2    Soland, F.3    Howald, H.4    Schaub, M.C.5
  • 8
    • 0030068816 scopus 로고    scopus 로고
    • Enhanced electrophoretic separation and resolution of myosin heavy chains in mammalian and avian skeletal muscles
    • Blough E.R., Rennie E.R., Zhang F., and Reiser P.J. Enhanced electrophoretic separation and resolution of myosin heavy chains in mammalian and avian skeletal muscles. Anal. Biochem. 233 (1996) 31-35
    • (1996) Anal. Biochem. , vol.233 , pp. 31-35
    • Blough, E.R.1    Rennie, E.R.2    Zhang, F.3    Reiser, P.J.4
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of dye-binding
    • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of dye-binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 10
    • 0014838245 scopus 로고
    • Three myosin ATPase systems: the nature of their pH lability and sulfhydryl dependence
    • Brooke M.H., and Kaiser K.K. Three myosin ATPase systems: the nature of their pH lability and sulfhydryl dependence. J. Histochem. Cytochem. 18 (1970) 670-672
    • (1970) J. Histochem. Cytochem. , vol.18 , pp. 670-672
    • Brooke, M.H.1    Kaiser, K.K.2
  • 11
    • 0942300427 scopus 로고    scopus 로고
    • Myosin heavy chain isoforms expressed in bovine skeletal muscles
    • Chikuni K., Muroya S., and Nakajima I. Myosin heavy chain isoforms expressed in bovine skeletal muscles. Meat Sci. 67 (2004) 87-94
    • (2004) Meat Sci. , vol.67 , pp. 87-94
    • Chikuni, K.1    Muroya, S.2    Nakajima, I.3
  • 12
    • 0036176023 scopus 로고    scopus 로고
    • Quantifying the temporospatial expression of postnatal porcine skeletal myosin heavy chain genes
    • da Costa N., Blackley R., Alzuherri H., and Chang K.C. Quantifying the temporospatial expression of postnatal porcine skeletal myosin heavy chain genes. J. Histochem. Cytochem. 50 (2002) 353-364
    • (2002) J. Histochem. Cytochem. , vol.50 , pp. 353-364
    • da Costa, N.1    Blackley, R.2    Alzuherri, H.3    Chang, K.C.4
  • 13
    • 0018729586 scopus 로고
    • An electrophoretic study of native myosin isozymes and of their subunit content
    • D'Albis A., Pantaloni C., and Bechet J.J. An electrophoretic study of native myosin isozymes and of their subunit content. Eur. J. Biochem. 99 (1979) 261-272
    • (1979) Eur. J. Biochem. , vol.99 , pp. 261-272
    • D'Albis, A.1    Pantaloni, C.2    Bechet, J.J.3
  • 14
    • 0034387980 scopus 로고    scopus 로고
    • Specificity of different anti-myosin heavy chain antibodies in bovine muscle
    • Duris M.-P., Picard B., and Geay Y. Specificity of different anti-myosin heavy chain antibodies in bovine muscle. Meat Sci. 55 (2000) 67-78
    • (2000) Meat Sci. , vol.55 , pp. 67-78
    • Duris, M.-P.1    Picard, B.2    Geay, Y.3
  • 15
    • 0023873317 scopus 로고
    • Maximum velocity of shortening related to myosin isoform composition in frog skeletal muscle fibres
    • Edman K.A., Reggiani C., Schiaffino S., and Te Kronnie G. Maximum velocity of shortening related to myosin isoform composition in frog skeletal muscle fibres. J. Physiol. 395 (1988) 679-694
    • (1988) J. Physiol. , vol.395 , pp. 679-694
    • Edman, K.A.1    Reggiani, C.2    Schiaffino, S.3    Te Kronnie, G.4
  • 16
    • 0020452557 scopus 로고
    • Variability of fiber type distributions within human muscles
    • Elder G.C., Bradbury K., and Roberts R. Variability of fiber type distributions within human muscles. J. Appl. Physiol. 53 (1982) 1473-1480
    • (1982) J. Appl. Physiol. , vol.53 , pp. 1473-1480
    • Elder, G.C.1    Bradbury, K.2    Roberts, R.3
  • 17
    • 0036090026 scopus 로고    scopus 로고
    • Development of sex differences in the rabbit masseter muscle is not restricted to a critical period
    • English A.W., and Schwartz G. Development of sex differences in the rabbit masseter muscle is not restricted to a critical period. J. Appl. Physiol. 92 (2002) 1214-1222
    • (2002) J. Appl. Physiol. , vol.92 , pp. 1214-1222
    • English, A.W.1    Schwartz, G.2
  • 18
    • 0031825365 scopus 로고    scopus 로고
    • Different phenotypes among slow/beta myosin heavy chain-containing fibres of rabbit masseter muscle: a novel type of diversity in adult muscle
    • English A.W., Eason J., Pol M., Schwartz G., and Shirley A. Different phenotypes among slow/beta myosin heavy chain-containing fibres of rabbit masseter muscle: a novel type of diversity in adult muscle. J. Muscle Res. Cell Motil. 19 (1998) 525-535
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 525-535
    • English, A.W.1    Eason, J.2    Pol, M.3    Schwartz, G.4    Shirley, A.5
  • 19
    • 0010933224 scopus 로고
    • Skeletal muscle characteristics of reindeer (Rangifer tarandus L.)
    • Essén-Gustavsson B., and Rehbinder C. Skeletal muscle characteristics of reindeer (Rangifer tarandus L.). Comp. Biochem. Physiol. A 82 (1985) 675-679
    • (1985) Comp. Biochem. Physiol. A , vol.82 , pp. 675-679
    • Essén-Gustavsson, B.1    Rehbinder, C.2
  • 20
    • 0024402489 scopus 로고
    • Factors affecting polyacrylamide gel electrophoresis and electroblotting of high-molecular-weight myofibrillar proteins
    • Fritz J.D., Swartz D.R., and Greaser M.L. Factors affecting polyacrylamide gel electrophoresis and electroblotting of high-molecular-weight myofibrillar proteins. Anal. Biochem. 180 (1989) 205-210
    • (1989) Anal. Biochem. , vol.180 , pp. 205-210
    • Fritz, J.D.1    Swartz, D.R.2    Greaser, M.L.3
  • 22
    • 0034918397 scopus 로고    scopus 로고
    • Evidence for three fast myosin heavy chain isoforms in type ii skeletal muscle fibers in the adult llama (Lama glama)
    • Graziotti G.H., Rios C.M., and Rivero J.L. Evidence for three fast myosin heavy chain isoforms in type ii skeletal muscle fibers in the adult llama (Lama glama). J. Histochem. Cytochem. 49 (2001) 1033-1044
    • (2001) J. Histochem. Cytochem. , vol.49 , pp. 1033-1044
    • Graziotti, G.H.1    Rios, C.M.2    Rivero, J.L.3
  • 23
    • 33745669302 scopus 로고    scopus 로고
    • Game and venison - meat for the modern consumer
    • Hoffman L.C., and Wiklund E. Game and venison - meat for the modern consumer. Meat Sci. 74 (2006) 197-208
    • (2006) Meat Sci. , vol.74 , pp. 197-208
    • Hoffman, L.C.1    Wiklund, E.2
  • 24
    • 0018637221 scopus 로고
    • Rabbit skeletal myosin isoenzymes from fetal, fast-twitch and slow-twitch muscles
    • Hoh J.F., and Yeoh G.P. Rabbit skeletal myosin isoenzymes from fetal, fast-twitch and slow-twitch muscles. Nature 280 (1979) 321-323
    • (1979) Nature , vol.280 , pp. 321-323
    • Hoh, J.F.1    Yeoh, G.P.2
  • 25
    • 0023182392 scopus 로고
    • Fiber composition and capillarity in growing guinea pigs acclimated to cold and cold plus hypoxia
    • Jackson C.G., Sillau A.H., and Banchero N. Fiber composition and capillarity in growing guinea pigs acclimated to cold and cold plus hypoxia. Proc. Soc. Exp. Biol. Med. 185 (1987) 101-106
    • (1987) Proc. Soc. Exp. Biol. Med. , vol.185 , pp. 101-106
    • Jackson, C.G.1    Sillau, A.H.2    Banchero, N.3
  • 26
    • 17444401012 scopus 로고    scopus 로고
    • Age-related changes in metabolic properties of equine skeletal muscle associated with muscle plasticity
    • Kim J.S., Hinchcliff K.W., Yamaguchi M., Beard L.A., Markert C.D., and Devor S.T. Age-related changes in metabolic properties of equine skeletal muscle associated with muscle plasticity. Vet. J. 169 (2005) 397-403
    • (2005) Vet. J. , vol.169 , pp. 397-403
    • Kim, J.S.1    Hinchcliff, K.W.2    Yamaguchi, M.3    Beard, L.A.4    Markert, C.D.5    Devor, S.T.6
  • 29
    • 34347207981 scopus 로고    scopus 로고
    • Electrophoretic separation of human skeletal muscle myosin heavy chain isoforms: the importance of reducing agents
    • Kohn T.A., and Myburgh K.H. Electrophoretic separation of human skeletal muscle myosin heavy chain isoforms: the importance of reducing agents. J. Physiol. Sci. 56 (2006) 355-360
    • (2006) J. Physiol. Sci. , vol.56 , pp. 355-360
    • Kohn, T.A.1    Myburgh, K.H.2
  • 30
    • 5744230364 scopus 로고    scopus 로고
    • Characteristics of impala (Aepyceros melampus) skeletal muscles
    • Kohn T.A., Kritzinger B., Hoffman L.C., and Myburgh K.H. Characteristics of impala (Aepyceros melampus) skeletal muscles. Meat Sci. 69 (2005) 277-282
    • (2005) Meat Sci. , vol.69 , pp. 277-282
    • Kohn, T.A.1    Kritzinger, B.2    Hoffman, L.C.3    Myburgh, K.H.4
  • 31
    • 0038168969 scopus 로고    scopus 로고
    • Myosin heavy-chain isoform composition of human single jaw-muscle fibers
    • Korfage J.A., and Van Eijden T.M. Myosin heavy-chain isoform composition of human single jaw-muscle fibers. J. Dent. Res. 82 (2003) 481-485
    • (2003) J. Dent. Res. , vol.82 , pp. 481-485
    • Korfage, J.A.1    Van Eijden, T.M.2
  • 32
    • 0031024917 scopus 로고    scopus 로고
    • A rapid electrophoretic method for separating rabbit skeletal-muscle myosin heavy-chains at high-resolution
    • Kubis H.P., and Gros G. A rapid electrophoretic method for separating rabbit skeletal-muscle myosin heavy-chains at high-resolution. Electrophoresis 18 (1997) 64-66
    • (1997) Electrophoresis , vol.18 , pp. 64-66
    • Kubis, H.P.1    Gros, G.2
  • 33
    • 0027763495 scopus 로고
    • Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles
    • Larsson L., and Moss R.L. Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles. J. Physiol. 472 (1993) 595-614
    • (1993) J. Physiol. , vol.472 , pp. 595-614
    • Larsson, L.1    Moss, R.L.2
  • 34
    • 0026195858 scopus 로고
    • Influence of environmental temperature on growth, muscle and adipose tissue metabolism, and meat quality in swine
    • Lefaucheur L., Le Dividich J., Mourot J., Monin G., Ecolan P., and Krauss D. Influence of environmental temperature on growth, muscle and adipose tissue metabolism, and meat quality in swine. J. Anim. Sci. 69 (1991) 2844-2854
    • (1991) J. Anim. Sci. , vol.69 , pp. 2844-2854
    • Lefaucheur, L.1    Le Dividich, J.2    Mourot, J.3    Monin, G.4    Ecolan, P.5    Krauss, D.6
  • 37
    • 21744457279 scopus 로고    scopus 로고
    • Myosin heavy chain 2B isoform is expressed in specialized eye muscles but not in trunk and limb muscles of cattle
    • Maccatrozzo L., Patruno M., Toniolo L., Reggiani C., and Mascarello F. Myosin heavy chain 2B isoform is expressed in specialized eye muscles but not in trunk and limb muscles of cattle. Eur. J. Histochem. 48 (2004) 357-366
    • (2004) Eur. J. Histochem. , vol.48 , pp. 357-366
    • Maccatrozzo, L.1    Patruno, M.2    Toniolo, L.3    Reggiani, C.4    Mascarello, F.5
  • 38
    • 33745829431 scopus 로고    scopus 로고
    • Scaling of skeletal muscle shortening velocity in mammals representing a 100,000-fold difference in body size
    • Marx J.O., Olsson M.C., and Larsson L. Scaling of skeletal muscle shortening velocity in mammals representing a 100,000-fold difference in body size. Pflügers Arch. 452 (2006) 222-230
    • (2006) Pflügers Arch. , vol.452 , pp. 222-230
    • Marx, J.O.1    Olsson, M.C.2    Larsson, L.3
  • 40
    • 0031893185 scopus 로고    scopus 로고
    • Electrophoretic separation and quantitation of cardiac myosin heavy-chain isoforms in 8 mammalian-species
    • Reiser P.J., and Kline W.O. Electrophoretic separation and quantitation of cardiac myosin heavy-chain isoforms in 8 mammalian-species. Am. J. Physiol. 43 (1998) H1048-H1053
    • (1998) Am. J. Physiol. , vol.43
    • Reiser, P.J.1    Kline, W.O.2
  • 41
    • 0022252990 scopus 로고
    • Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition
    • Reiser P.J., Moss R.L., Giulian G.G., and Greaser M.L. Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition. J. Biol. Chem. 260 (1985) 9077-9080
    • (1985) J. Biol. Chem. , vol.260 , pp. 9077-9080
    • Reiser, P.J.1    Moss, R.L.2    Giulian, G.G.3    Greaser, M.L.4
  • 43
    • 0030726921 scopus 로고    scopus 로고
    • A sensitive electrophoretic method for the quantification of myosin heavy chain isoforms in horse skeletal muscle: histochemical and immunocytochemical verifications
    • Rivero J.L.L., Talmadge R.J., and Edgerton V.R. A sensitive electrophoretic method for the quantification of myosin heavy chain isoforms in horse skeletal muscle: histochemical and immunocytochemical verifications. Electrophoresis 18 (1997) 1967-1972
    • (1997) Electrophoresis , vol.18 , pp. 1967-1972
    • Rivero, J.L.L.1    Talmadge, R.J.2    Edgerton, V.R.3
  • 44
    • 0035317867 scopus 로고    scopus 로고
    • Effects of treadmill speed on the mechanics of the back in the trotting saddlehorse
    • Suppl.
    • Robert C., Audigie F., Valette J.P., Pourcelot P., and Denoix J.M. Effects of treadmill speed on the mechanics of the back in the trotting saddlehorse. Equine Vet. J. (2001) 154-159 Suppl.
    • (2001) Equine Vet. J. , pp. 154-159
    • Robert, C.1    Audigie, F.2    Valette, J.P.3    Pourcelot, P.4    Denoix, J.M.5
  • 45
    • 23944481844 scopus 로고    scopus 로고
    • Identification of myosin heavy chain I, IIa and IIx in canine skeletal muscles by an electrophoretic and immunoblotting study
    • Smerdu V., Strbenc M., Meznaric-Petrusa M., and Fazarinc G. Identification of myosin heavy chain I, IIa and IIx in canine skeletal muscles by an electrophoretic and immunoblotting study. Cells Tissues Organs 180 (2005) 106-116
    • (2005) Cells Tissues Organs , vol.180 , pp. 106-116
    • Smerdu, V.1    Strbenc, M.2    Meznaric-Petrusa, M.3    Fazarinc, G.4
  • 47
    • 0018630107 scopus 로고
    • Comparative aspects of muscle fibre size and succinic dehydrogenase distribution in the longissimus dorsi muscle of several species of East African mammals
    • Stickland N.C. Comparative aspects of muscle fibre size and succinic dehydrogenase distribution in the longissimus dorsi muscle of several species of East African mammals. Acta Anat. 105 (1979) 381-385
    • (1979) Acta Anat. , vol.105 , pp. 381-385
    • Stickland, N.C.1
  • 48
    • 0027452352 scopus 로고
    • Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms
    • Talmadge R.J., and Roy R.R. Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms. J. Appl. Physiol. 75 (1993) 2337-2340
    • (1993) J. Appl. Physiol. , vol.75 , pp. 2337-2340
    • Talmadge, R.J.1    Roy, R.R.2
  • 50
    • 29044449641 scopus 로고    scopus 로고
    • Expression of eight distinct MHC isoforms in bovine striated muscles: evidence for MHC-2B presence only in extraocular muscles
    • Toniolo L., Maccatrozzo L., Patruno M., Caliaro F., Mascarello F., and Reggiani C. Expression of eight distinct MHC isoforms in bovine striated muscles: evidence for MHC-2B presence only in extraocular muscles. J. Exp. Biol. 208 (2005) 4243-4253
    • (2005) J. Exp. Biol. , vol.208 , pp. 4243-4253
    • Toniolo, L.1    Maccatrozzo, L.2    Patruno, M.3    Caliaro, F.4    Mascarello, F.5    Reggiani, C.6
  • 52
    • 3042695007 scopus 로고    scopus 로고
    • Human single muscle fibre function with 84 day bed-rest and resistance exercise
    • Trappe S., Trappe T., Gallagher P., Harber M., Alkner B., and Tesch P. Human single muscle fibre function with 84 day bed-rest and resistance exercise. J. Physiol. 557 (2004) 501-513
    • (2004) J. Physiol. , vol.557 , pp. 501-513
    • Trappe, S.1    Trappe, T.2    Gallagher, P.3    Harber, M.4    Alkner, B.5    Tesch, P.6
  • 53
    • 0032527977 scopus 로고    scopus 로고
    • Fast to slow transformation of denervated and electrically stimulated rat muscle
    • Windisch A., Gundersen K., Szabolcs M.J., Gruber H., and Lomo T. Fast to slow transformation of denervated and electrically stimulated rat muscle. J. Physiol. 510 (1998) 623-632
    • (1998) J. Physiol. , vol.510 , pp. 623-632
    • Windisch, A.1    Gundersen, K.2    Szabolcs, M.J.3    Gruber, H.4    Lomo, T.5
  • 54
    • 0010906688 scopus 로고
    • Cattle at risk for dark-cutting beef have a higher proportion of oxidative muscle-fibers
    • Zerouala A.C., and Stickland N.C. Cattle at risk for dark-cutting beef have a higher proportion of oxidative muscle-fibers. Meat Sci. 29 (1991) 263-270
    • (1991) Meat Sci. , vol.29 , pp. 263-270
    • Zerouala, A.C.1    Stickland, N.C.2


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