Hostname: page-component-586b7cd67f-vdxz6 Total loading time: 0 Render date: 2024-11-29T03:46:07.208Z Has data issue: false hasContentIssue false
  • English
  • Français

Effect of exercise during rehabilitation on swimming performance, metabolism and function of muscle in rats

Published online by Cambridge University Press:  09 March 2007

N. V. Raju
N. V. Raju
Affiliation:
National Institute of Nutrition, Indian Council of Medical Research, Jamai-Osmania, Hyderabad-500007, India
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

1. It has been observed previously that gastrocnemius muscles from rats rehabilitated after early nutritional stress have low endurance and oxidative capacity (Raju, 1974).

2. Exercise during rehabilitation reversed the effects of early malnutrition on muscle function and metabolism. The swimming performance of rehabilitated rats was poor and exercise during rehabilitation improved it.

3. The specific activity of gastrocnemius muscle myosin ATP phosphohydrolase (EC 3.6.1.3) was not altered by either early malnutrition or exercise.

Type
Research Article
Information
British Journal of Nutrition , Volume 38 , Issue 2 , September 1977 , pp. 157 - 165
Copyright
Copyright © The Nutrition Society 1977

References

Astrand, P. O. & Rodahl, K. (1970). Textbook of Work Physiology, p. 292,New York: Mcgraw-Hill.Google Scholar
Baldwin, K. M., Klinkerfuss, G. H., Terjung, R. L., Mole, P. A. & Holloszy, J. O. (1972). Am. J. Physiol. 222, 373.CrossRefGoogle Scholar
Baldwin, K. M., Winder, W. W., Terjung, R. L. & Holloszy, J. O. (1973). Am. J. Physiol. 225, 962.CrossRefGoogle Scholar
Barany, M. (1967). J. gen. Physiol. 50, 197.CrossRefGoogle Scholar
Barany, M., Barany, K., Reckard, T. & Volpe, A. (1965). Archs Biochem. Biophys. 109, 185.CrossRefGoogle Scholar
Barnard, R. J., Edgerton, V. R. & Peter, J. B. (1970). J. appl. Physiol. 28, 762.CrossRefGoogle Scholar
Barnard, R. J., Edgerton, V. R., Furukawa, T. & Peter, J. B. (1971). Am. J. Physiol. 220, 410.CrossRefGoogle Scholar
Barnard, R. J. & Peter, J. B. (1971). J. appl. Physiol. 31, 904.CrossRefGoogle Scholar
Barnes, R. H. (1971). Fedn Proc. Fedn Am. Socs exp. Biol. 30, 1429.Google Scholar
Close, R. (1972). Physiol. Rev. 52, 129.CrossRefGoogle Scholar
Dohm, G. L., Huston, R. L., Askew, W. E. S., Fleshood, L. H. (1973). Can. J. Biochem. 51, 849.CrossRefGoogle Scholar
Faulkner, J. A., Maxwell, L. C., Brook, D. A. & Lieberman, D. H. (1971). Am. J. Physiol. 221, 291.CrossRefGoogle Scholar
Frankova, S. & Barnes, R. H. (1968). J. Nutr. 96, 477.CrossRefGoogle Scholar
Fuge, K. W., Crews, E. L., Pattengale, P. K., Holloszy, J. O. & Shank, R. E. (1968). Am. J. Physiol. 215 660.CrossRefGoogle Scholar
Gordon, E. E., Kowalski, K. & Fritts, M. (1966). Am. J. Physiol. 210, 1033.CrossRefGoogle Scholar
Gould, M. K. & Rawlinson, W. A. (1959). Biochem. J. 73, 41.CrossRefGoogle Scholar
Hearn, G. R. & Wainio, W. W. (1956). Am. J. Physiol. 185, 348.CrossRefGoogle Scholar
Holloszy, J. O. (1967). J. biol. Chem. 242, 2278.CrossRefGoogle Scholar
Holloszy, J. O., Oscai, L. B., Don, T. J. & Mole, P. A. (1971). Biochem. Biophys. Res. Commun. 40, 1368.CrossRefGoogle Scholar
Kennedy, G. C. (1957). J. Endocrinol. 15, 9.CrossRefGoogle Scholar
Kornberg, A. (1955). Meth. Enzym. 1, 441.CrossRefGoogle Scholar
Mcardle, W. D. & Montoye, H. J. (1966). J. appl. Physiol. 21, 1431.CrossRefGoogle Scholar
Montoye, H. J., Nelson, R., Johnson, P. & Macnab, R. (1960). Res. Am. Ass. Hlth phys. Educ. 31,474.Google Scholar
National Academy of Sciences – National Research Council (1963). Evaluation of Protein Quality, publ. no. 1100. Washington, DC: National Academy of Sciences.Google Scholar
Ochoa, S. (1955). Meth. Enzym. 1, 735.CrossRefGoogle Scholar
Perry, S. V. (1973). In The physiology and Biochemistry of Muscle as a Food, Vol. 2, p. 537 [Briskley, E. J., Gassens, R. G. and Marsch, B. R., editors]. Wisconsin: University of Wisconsin Press.Google Scholar
Pette, D., Smith, M. E., Staudte, H. W. & Vrbova, G. (1973). Pflugers Arch. ges. Physiol. 338, 287.CrossRefGoogle Scholar
Pette, D., Staudte, H. W. & Vrbova, G. (1972). Naturwissenschaften 59, 469.CrossRefGoogle Scholar
Raju, N. V. (1974). Life Sci. 15, 949.CrossRefGoogle Scholar
Riley, D. A. & Allin, E. F. (1973). Expl Neurol. 40, 391.CrossRefGoogle Scholar
Siedel, J. C. (1967). J. biol. Chem. 242, 5623.CrossRefGoogle Scholar
Syrovy, I., Gutman, E. & Melichna, J. (1972). Physiologia Bohemosloy, 21, 638.Google Scholar
Taylor, J. F. (1955). Meth. Enzym. 1, 310.CrossRefGoogle Scholar
Torun, B., Schutz, Y., Bradfield, R. & Viteri, F. E. (1975). In Abstracts of Xth International Congress of Nutrition, abstr. no. 314, p. 29 [Koishi, H., Hosoya, N. and Yasumoto, K., editors]. Kyoto: Science Council of Japan.Google Scholar
Trayer, J. P. & Perry, S. V. (1966). Biochem. Z. 345, 57.Google Scholar
Wesson, L. G. (1952). Science, N.Y. 75, 339.CrossRefGoogle Scholar