Human soleus muscle: A comparison of fiber composition and enzyme activities with other leg muscles


The relationship between fiber composition and enzyme profiles as estimated from in vitro enzyme activities has been studied in human skeletal muscle. Samples from the soleus, gastrocnemius, and vastus lateralis muscles were obtained both by biopsying normal subjects and from patients during nonmuscular related general surgery. The samples were analyzed for fiber composition, phosphorylase (a+b), phosphofructokinase, and creatine phosphokinase activities. The fibers were assigned to two major types based on the histochemical display of alkaline stable myofibrillar adenosine triphosphatase staining. This staining is related to the activity of the enzyme and thus the contractility of the fibers. One fibre type lacks (Type I or slow twitch fiber) and the other one (Type II or fast twitch fiber) contains this enzyme. The soleus muscle contained predominantly slow twitch (Type I) fibers with the mean for all subjects being 80% (range 64 to 100%). In contrast the gastrocnemius and vastus lateralis muscles only contained 57% slow twitch fibers (range 34–82%). The activities of the glycolytic enzymes assayed, except hexokinase, were lower in predominantly slow twitch as compared with muscle with many fast twitch fibers and this was consistent with muscle histochemical staining patterns for alpha glycerophosphate dehydrogenase. Succinate dehydrogenase and creatine phosphokinase activities were not related to fiber distribution.

This is a preview of subscription content, log in to check access.


  1. 1.

    Baldwin, K. J., Klinkerfuß, G. H., Terjung, R. L., Molé, P. A., Holloszy, L. O.: Respiratory capacity of white, red, and intermediate muscle: adaptative response to exercise. Amer. J. Physiol.222, 373–378 (1972)

    Google Scholar 

  2. 2.

    Baldwin, K. M., Winder, W. W., Terjung, R. L., Holloszy, J. O.: Glycolytic enzymes in different types of skeletal muscle: adaptation to exercise. Amer. J. Physiol.225, 962–966 (1973)

    Google Scholar 

  3. 3.

    Bárány, M.: ATPase activity of myosin correlated with speed of muscle shortening. J. gen. Physiol.50, 197–215 (1967).

    Google Scholar 

  4. 4.

    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, 410–415 (1971)

    Google Scholar 

  5. 5.

    Bergström, J.: Muscle electrolytes in man. Scand. J. clin. Lab. Invest., Suppl.68 (1962)

  6. 6.

    Buchthal, F., Dahl, K., Rosenfalck, P.: Rise time of the spike in fast and slow contracting muscle of man. Acta physiol. scand.87, 261–269 (1973)

    Google Scholar 

  7. 7.

    Buchthal, F., Schmalbruch, H.: Contraction times and fibre types in intact human muscle. Acta physiol. scand.79, 435–452 (1970)

    Google Scholar 

  8. 8.

    Cooperstein, S. J., Lazarow, A., Kurfess, N. J.: A microspectrophotometric method for the determination of succinic dehydrogenase. J. biol. Chem.186, 129–139 (1950)

    Google Scholar 

  9. 9.

    Dubowitz, B., Pearse, A. G. E.: A comparative histochemical study of oxidative enzymes and phosphorylase activity in skeletal muscle. Histochemie2, 105–117 (1960)

    Google Scholar 

  10. 10.

    Eberstein, A., Goodgold, J.: Slow and fast twitch fibers in human skeletal muscle. Amer. J. Physiol.215, 535–541 (1968)

    Google Scholar 

  11. 11.

    Edström, L.: Histochemical changes in upper motor lesions, parkinsonism and disuse. Differential effect on white and red muscle fibres. Experientia (Basel)24, 916–918 (1968)

    Google Scholar 

  12. 12.

    Edström, L., Ekblom, B.: Differences in size of red and white muscle fibres in vastus lateralis of m. quadriceps femoris of normal individuals and athletes. Scand. J. clin. Lab. Invest.30, 175–181 (1972)

    Google Scholar 

  13. 13.

    Edström, L., Nyström, B.: Histochemical types and sizes of fibres in normal human muscles. Acta neurol. scand.45, 257–269 (1969)

    Google Scholar 

  14. 14.

    Engel, W. K.: The multiplicity of pathological reactions in human skeletal muscle. Proc. Intern. Congr. Neuropathol. 5th, New York, 1966, pp. 613–624

  15. 15.

    Engel, W. K., Brooke, N. H., Nelson, P. G.: Histochemical studies of denervated or tenotomized cat muscle illustrating difficulties in relating experimental animal conditions to human neuromuscular diseases. Ann. N. Y. Acad. Sci.138, 160–185 (1966)

    Google Scholar 

  16. 16.

    Gollnick, P. D., Armstrong, R. B., Saltin, B., Saubert IV, C. W., Sembrowich, W. L., Shepherd, R. E.: Effect of training on enzyme activity and fiber composition of human skeletal muscle. J. appl. Physiol.34, 107–111 (1973)

    Google Scholar 

  17. 17.

    Gollnick, P. D., Armstrong, R. B., Saubert IV, C. W., Piehl, K., Saltin, B.: Enzyme activity and fiber composition in skeletal muscle of untrained and trained men. J. appl. Physiol.33, 312–319 (1972)

    Google Scholar 

  18. 18.

    Johnson, M. A., Polgar, J., Weightman, D., Appleton, D.: Data on the distribution of fibre types in thirty-six human muscles: an autopsy study. J. neurol. Sci.18, 111–129 (1973)

    Google Scholar 

  19. 19.

    Karlsson, J., Diamant, B., Saltin, B.: Lactate dehydrogenase activity in muscle after prolonged severe exercise in man. J. appl. Physiol.25, 88–91 (1968)

    Google Scholar 

  20. 20.

    Lowry, O. H., Passonneau, J. V.: The relationship between substrates and enzymes of glycolysis in brain. J. biol. Chem.239, 31–42 (1964)

    Google Scholar 

  21. 21.

    Lowry, O. H., Schulz, D. W., Passonneau, J. V.: Effect of adenylic acid on the kinetics of muscle phosphorylase a. J. biol. Chem.239, 1947–1953 (1964)

    Google Scholar 

  22. 22.

    Novikoff, A. B., Shin, W., Drucker, J.: Mitochondrial localization of oxidation enzymes: staining results with two tetrazolium salts. J. biophys. biochem. Cytol.9, 47–61 (1961)

    Google Scholar 

  23. 23.

    Padykula, H. A., Herman, E.: The specificity of the histochemical method of adenosine triphosphatase. J. Histochem. Cytochem.3, 170–195 (1955)

    Google Scholar 

  24. 24.

    Pearse, A. G. E.: Histochemistry-Theoretical and Applied, Appendix 9, p. 832. Boston, Mass.: Little, Brown 1961

    Google Scholar 

  25. 25.

    Pette, D.: Metabolic differentiation of distinct muscle types at the level of enzymatic organization. In: Muscle metabolism during exercise, B. Pernow and B. Saltin, Eds., pp. 33–49. New York: Plenum Press 1971

    Google Scholar 

  26. 26.

    Shonk, C. E., Boxer, G. E.: Enzyme patterns in human tissue. I. Methods for the determination of glycolytic enzymes. Cancer Res.24, 709–724 (1964)

    Google Scholar 

  27. 27.

    Sica, R. E. P., McComas, A. J.: Fast and slow twitch units in a human muscle. J. Neurol. Neurosurg. Psychiat.34, 113–120 (1971)

    Google Scholar 

  28. 28.

    Waternberg, L. W., Leong, J. L.: Effect of coenzyme Q10 and menadione on succinate dehydrogenase activity as measured by tetrazolium salt reduction. J. Histochem. Cytochem.8, 269–303 (1960)

    Google Scholar 

Download references

Author information



Rights and permissions

Reprints and Permissions

About this article

Cite this article

Gollnick, P.D., Sjödin, B., Karlsson, J. et al. Human soleus muscle: A comparison of fiber composition and enzyme activities with other leg muscles. Pflugers Arch. 348, 247–255 (1974).

Download citation

Key words

  • Phosphorylase
  • Lactate Dehydrogenase
  • Succinate Dehydrogenase
  • Fiber Composition and Enzyme Activities
  • Phosphofructokinase
  • Human Muscle Characteristics