Summary
The myosin content from red and white muscles of three marine fish species, saithe (Pollachius virens. L), haddock (Melanogrammus aeglefinus, L.), both members of the familyGadidae, and capeline (Mallotus villosus, M.) of the familyOsmeridae, was analyzed electrophoretically.
Analysis of the native myosin by electrophoresis under non-dissociating conditions revealed two isoforms in red muscles, and three or four in white muscles. The white muscles of the two closely related species had a similar pattern of isoforms.
Myosin from the slow red muscles had two types of light chain, LC1S and LC2S, and myosin from the fast white muscles three, LC1F, LC2F, and LC3F. The pattern of light chains in both types of muscles was species-dependent. All the light chains from fish myosins were more acidic than those of the rat diaphragm used as standard.
One main type of heavy chain was detected in each kind of muscle. In white muscles of saithe there was an extra band, present in minor amounts. The heavy chains from white muscle myosin had lower electrophoretic mobilities than those from red muscle, and the mobilities of all of them were intermediate between those of the heavy chains type IIa and I of rat diaphragm myosin.
In our opinion, there are probably more isomyosins in fish muscles than those detected in the present work and their presence is obscured by comigration with the main types.
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References
d'Albis, A., Couteaux, R., Janmot, C., &Mira, J. C. (1989) Myosin isoform transitions in regeneration of fast and slow muscles during postnatal development of the rat.Dev. Biol. 135, 320–5.
d'Albis, A., Janmot, C., Béchet, J.-J. (1985) Myosin switches in skeletal muscle development of an urodelan amphibian,Pleurodeles waltlii. Comparison with a mammalian,Mus musculus. Biochem. Biophys. Res. Commun. 128, 94–100.
d'Albis, A., Pantaloni, C. &BÉchet, J.-J. (1979) An electrophoretic study of native myosin isoenzymes and their subunit content.Eur. J. Biochem. 99, 261–72.
Anderson, C. W., Baum, P. R. &Gesteland, R. F. (1973) Processing of adenovirus 2-induced proteins.J. Virol. 12, 241–52.
Ansorge, W. (1983) Fast visualization of protein bands by impregnation in potassium permanganate and silver nitrate. InElectrophoresis' 82 (edited byStathakos, D.), pp. 235–42. Berlin, New York: Walter de Gruyter & Co.
Bone, Q. (1978) Locomotor muscle. InFish Physiology (edited byHoar, W. S. &Randall, D. J.), pp. 361–424. New York: Academic Press.
Bradford, M. M. (1976) A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.Anal. Biochem. 72, 248–54.
Carraro, U. &Catani, C. (1983) A sensitive SDS-PAGE method separating myosin heavy chain isoforms of rat skeletal muscles reveals the heterogeneous nature of the embryonic myosin.Biochem. Biophys. Res. Commun. 116, 793–802.
Focant, B., Huriaux, F. &Johnston, I. A. (1976) Subunit composition of fish myofibrils: the light chains of myosin.Int. J. Biochem. 7, 129–33.
Hoh, J. F. Y. (1979) Development changes in chicken skeletal myosin isoenzymes.FEBS Lett. 98, 267–70.
Hoh, J. F. Y., McGrath, P. A. &White, R. I. (1976) Electrophoretic analysis of multiple forms of myosin in fast-twitch and slow-twitch muscles of the chick.Biochem. J. 157, 87–95.
Huriaux, F. &Focant, B. (1978) Effect of some factors on the molecular weight determinations of a light chain (LC3) of carp (Cyprinus carpio L.) skeletal muscle myosin by SDSpolyacrylamide gel electrophoresis.Comp. Biochem. Physiol. 61B, 195–8.
Huriaux, F. &Focant, B. (1985) Electrophoretic and immunological study of myosin light chains from freshwater teleost fishes.Comp. Biochem. Physiol. 82B, 737–43.
Johnston, I. A. (1980) Specialisations of fish muscle. InDevelopment and Specialisation of Skeletal Muscle (edited byGoldspink, D. F.). Society Exp. Biol. Seminar Series. Vol.7, pp. 123–48. Cambridge: Cambridge University Press.
Johnston, I. A., Frearson, N. &Goldspink, G. (1972) Myofibrillar ATPase activities of red and white myotommal muscles of marine fish.Experientia 28, 713–4.
Johnston, I. A. &Moon, T. W. (1980) Exercise training in skeletal muscle of brook trout (Salvelinus fontinalis).J. exp. Biol. 87, 177–94.
Jolesz, F. &Sreter, F. A. (1981) Development, innervation, and activity induced changes in skeletal muscle.Ann. Rev. Physiol. 43, 531–52.
Karasinksi, J. &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, 727–31.
Korneliussen, H., Dhal, H. A. &Paulsen, J. E. (1978) Histochemical definition of muscle fibre types in the trunk musculature of a teleost fish (Cod,Gadus morhua, L).Histochemistry 55, 1–16.
Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4.Nature 227, 680–5.
Martinez, I., Olsen, R. L., Ofstad, R., Janmot, C. & d'Albis, A. (1989) Myosin isoforms in mackerel (Scomber scombrus) red and white muscles.FEBS Lett. 252, 69–72.
Martinez, I., Ofstad, R. &Olsen, R. L. (1990) Electrophoretic study of myosin isoforms in white muscles of some teleost fishes.Comp. Biochem. Physiol.,96B, 221–27.
Nag, A. C. &Nursall, J. R. (1972) Histogenesis of white and red muscle fibres of trunk muscles of a fishSalmo gairdneri.Cytobios 6, 227–46.
Ofarrell, P. H. (1975) High resolution two-dimensional electrophoresis of proteins.J. biol. Chem. 250, 4007–21.
Ochiai, Y., Kobayashi, T., Watabe, S. &Hashimoto, K. (1990) Mapping of fish myosin light chains by two-dimensional gel electrophoresis.Comp. Biochem. Physiol. 95B, 341–5.
Ochiai, Y., Watabe, S. &Hashimoto, K. (1988) Physicochemical and immunological properties of myosin light chains from the ordinary muscles of marine teleost fishes.Comp. Biochem. Physiol. 90B, 347–53.
Reiser, P. J., Moss, R. L., Giulian, G. G. &Greaser, M. L. (1985) Shortening velocity in single fibers from adult rabbit soleus muscle is correlated with myosin heavy chain composition.J. biol. Chem.,260, 263–74.
Rowlerson, A., Scapolo, P. A., Mascarello, F., Carpene, E. &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. Musc. Res. Cell Motil. 6, 601–40.
Scapolo, P. A. &Rowlerson, A. (1987) Pink lateral muscle in the carp (Cyprinus carpio L): Histochemical properties and myosin composition.Experientia 43, 384–6.
Schiaffino, S., Gorza, L., Sartore, S., Saggin, L., Ausoni, S., Vianello, M., Gundersen, C. &LØmo, T. (1989) Three myosin heavy chain isoforms in type 2 skeletal muscle fibres.J. Muscle Res. Cell Motil 10, 197–205.
Termin, A., Staron, R. S. &Pette, D. (1989) Myosin heavy chain isoforms in histochemically defined fibre types of the rat muscle.Histochemistry 92, 453–7.
Watabe, S.;Ochiai, Y. &Hashimoto, K. (1982) Identification of 5,5′-dithio-bis-2-nitrobenzoic acid (DTNB) and alkali light chains of piscine myosin.Nippon Suisan Gakkaishi 48, 827–32.
Whalen, R. G., Butler-Browne, G. S. &Gros, F. (1978) Identification of a novel form of myosin light chain present in embryonic muscle tissue and cultured muscle cells.J. Mol. Biol. 126, 415–31.
Whalen, R. G., Sell, S. M., Butler-Brown, G. S., Schwartz, K., Bouveret, P. &Pinset-Härström, I. (1981) Three myosins heavy chains isozymes appear sequentially in rat muscle development.Nature 292, 805–9.
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Martinez, I., Ofstad, R. & Olsen, R.L. Myosin isoforms in red and white muscles of some marine teleost fishes. J Muscle Res Cell Motil 11, 489–495 (1990). https://doi.org/10.1007/BF01745216
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DOI: https://doi.org/10.1007/BF01745216