Summary
Methods for standardized determination of phosphofructokinase (PFK), glyceraldehydephosphate dehydrogenase (GAPDH), lactate dehydrogenase (LDH) and malate dehydrogenase (MDH) activities in nanogram samples of microdissected single fibres of rabbit psoas and soleus muscle are described. Fast and slow fibres in soleus muscle show lower absolute activities of these enzymes than the respective fibre types in psoas muscle. Slow fibres represent a more uniform population in the two muscles according to absolute and relative activities of the enzymes investigated. Slow fibres are characterized by high activities of MDH and relatively low activities of glycolytic enzymes. Fast fibres in the soleus muscle represent a population with high activities of MDH and glycolytic enzymes. Fast fibres in psoas muscle represent a heterogeneous population with high activities of glycolytic enzymes and extremely variable activity of MDH. More than 10-fold differences exist in the MDH activities of the extreme types of this fibre population. Differences in the activity levels of MDH in single fast type fibres but also in the activities of glycolytic enzymes between fast and slow fibres are greater than those reported between extreme white and red rabbit muscles.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Bárány, M.: ATPase activity of myosin correlated with speed of muscle shortening. J. gen. Physiol. 50, (Suppl., part 2) 197–218 (1967)
Barnard, R.J., Edgerton, V.R., Furukawa, T., Peter, J.B.: Histochemical, biochemical, and contractile properties of red, white, and intermediate fibers. Amer. J. Physiol. 220, 410–414 (1971)
Bass, A., Brdiczka, D., Eyer, P., Hofer, S., Pette, D.: Metabolic differentiation of distinct muscle types at the level of enzymatic organization. Europ. J. Biochem. 10, 198–206 (1969)
Brown, M. D., Cotter, M.A., Hudlická, O., Vrbová, G.: The effects of different patterns of muscle activity on capillary density, mechanical properties and structure of slow and fast rabbit muscles. Pflügers Arch. 361, 241–250 (1976)
Bücher, T., Luh, W., Pette, D.: Einfache und zusammengesetzte optische Tests mit Pyridinnucleotiden. In: Handbuch der physiologisch- und pathologisch-chemischen Analyse Bd. VI/A (Hoppe-Seyler/Thierfelder, eds.), pp. 292–239. Berlin-Heidelberg-New York: Springer 1964
Burke, R.E., Tsairis, P., Levine, D.N., Zajac, F.E., III, Engel, W.L.: Direct correlation of physiological and histochemical characteristics in motor units of cat triceps surae muscle. In: New developments in electromyography and clinical neurophysiology (J.E. Desmedt, ed.), Vol. 1, pp. 23–30. Basel: Karger 1973
Close, R.I.: Dynamic properties of mammalian skeletal muscles. Physiol. Rev. 52, 129–197 (1972)
Dawson, D.M., Romanul, F.C.A.: Enzymes in muscle II. Histochemical and quantitative studies. Arch. Neurol. 11, 369–378 (1964)
Dickerson, J.W.T., Widdowson, E.M.: Chemical changes in skeletal muscle during development. Biochem. J. 74, 247–257 (1960)
Edström, L., Kugelberg, E.: Histochemical composition, distribution of fibres and fatiguability of single motor units. Anterior tibial muscle of the rat. J. Neurol. Neurosurg. Psychiat. 31, 424–433 (1968)
Essén, B., Jansson, E., Henriksson, J., Taylor, A.W., Saltin, B.: Metabolic characteristics of fibre types in human skeletal muscle. Acta physiol. scand. 95, 153–165 (1975)
Henneman, E., Olson, C.B.: Relations between structure and function in the design of skeletal muscle. J. Neurophysiol. 28, 581–598 (1965)
Khan, M.A.: Histochemical characteristics of vertebrate striated muscle — A Review. Progr. Histochem. Cytochem. 8, 1–47 (1976)
Lowey, S., Risby, D.: Light chains from fast and slow muscle myosins. Nature. (Lond.) 234, 81–85 (1971)
Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J.: Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265–275 (1951)
Lowry, O.H., Passonneau, J.V.: A flexible system of enzymatic analysis. New York and London: Academic Press 1972
Matschinsky, F.M., Passonneau, J.V., Lowry, O.H.: Quantitative histochemical analysis of glycolytic intermediates and cofactors with an oil well technique. J. Histochem. Cytochem. 16, 29–39 (1968)
Müller, W.: Temporal progress of muscle adaptation to endurance training in hind limb muscles of young rats. A histochemical and morphometrical study. Cell Tiss. Res. 156, 61–87 (1974)
Nelson, J.S., Tashiro, K.: The analysis of skeletal muscle by quantitative histochemical techniques. J. Neuropath. Exper. Neurol. 32, 371–379 (1973)
Nolte, J., Pette, D.: Microphotometric determination of enzymeactivity in single cells in cryostat sections. II. Succinate dehydrogenase, lactate dehydrogenase and triosephosphate dehydrogenase activities in red, intermediate and white fibers of soleus and rectus femoris muscle of rat. J. Histochem. Cytochem. 20, 577–582 (1972)
Padykula, H.A., Herman, E.: The specificity of the histochemical method for adenosine triphosphatase. J. Histochem. Cytochem. 3, 170–195 (1955)
Perrie, W.T., Perry, S.V.: An electrophoretic study of the low-molecular-weight components of myosin. Biochem. J. 119, 31–38 (1970)
Peter, J.B., Barnard, R.J., Edgerton, V.R., Gillespie, C.A., Stempel, K.E.: Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits. Biochemistry 11, 2627–2633 (1972)
Pette, D., Bücher, T.: Proportionskonstante Gruppen in Beziehung zur Differenzierung der Enzymaktivitätsmuster von Skelett-Muskeln des Kaninchens. Hoppe-Seylers Z. Physiol. Chem. 331, 180–195 (1963)
Pette, D.: Plan und Muster im zellulären Stoffwechsel. Naturwissenschaften 52, 597–616 (1965)
Pette, D., Staudte, H.W.: Differences between red and white muscles. In: Limiting factors of physical performance (J. Keul, ed.), pp. 23–35. Stuttgart: Thieme 1973
Pette, D., Smith, M.E., Staudte, H.W., Vrbová, G.: Effects of long-term electrical stimulation on some contractile and metabolic characteristics of fast rabbit muscles. Pflügers Arch. 338, 257–272 (1973)
Pette, D., Dölken, G.: Some aspects of regulation of enzyme levels in muscle energy-supplying metabolism. In: Advances in enzyme regulation (G. Weber, ed.), Vol. 13, pp. 355–377. Oxford and New York: Pergamon Press (1975)
Ranvier, L.: Propriétés et structures différentes des muscles rouges et des muscles blancs chez les lapins et chez les raies. C.R. Acad. Sci. (Paris) 77, 1030–1034 (1873)
Romanul, F.C.A., Sréter, F.A., Salmons, S., Gergely, J.: The effect of a changed pattern of activity on histochemical characteristics of muscle fibers. In: Exploratory concepts in muscular dystrophy II. Int. Congr. Ser. (A.T. Milhorat, ed.), 333, pp. 344–348. Amsterdam: Excerpta Medica 1974
Samaha, F.J., Guth, L., Albers, R.W.: Differences between slow and fast muscle myosin. Adenosine triphosphatase activity and release of associated proteins by p-chloromercuri-phenylsulfonate. J. Biol. Chem. 245, 219–224 (1970)
Sarkar, S., Sréter, F.A., Gergely, J.: Light chains of myosins from white, red and cardiac muscles. Proc. Nat. Acad. Sci. (USA) 68, 946–950 (1971)
Watzka, M.: “Weiße” und “rote” Muskeln. Z. mikrosk.-anat. Forsch. 45, 668–678 (1939)
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Spamer, C., Pette, D. Activity patterns of phosphofructokinase, glyceraldehydephosphate dehydrogenase, lactate dehydrogenase and malate dehydrogenase in microdissected fast and slow fibres from rabbit psoas and soleus muscle. Histochemistry 52, 201–206 (1977). https://doi.org/10.1007/BF00495857
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00495857