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Aldose reductase and sorbitol dehydrogenase in the muscle of Ascaris suum (Nematoda)

Published online by Cambridge University Press:  06 April 2009

M. M. Goil  and
R. P. Harpur
M. M. Goil
Affiliation:
Institute of Parasitology, McGill University, Macdonald College Post Office, P.Q., Canada HOA 1CO
R. P. Harpur
Affiliation:
Institute of Parasitology, McGill University, Macdonald College Post Office, P.Q., Canada HOA 1CO
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Summary

The muscle of Ascaris suum contains sorbitol dehydrogenase [EC 1.1.1. 14] and the apparent Km values indicate that the enzymefavours fructose formation. Aldose reductase [EC 1.1.1.21] is also present and like the mammalian enzyme it has a very high apparent Km for glucose. Possible functions of the sorbitol pathway in Ascaris muscle are discussed.

Type
Research Article
Information
Parasitology , Volume 77 , Issue 1 , August 1978 , pp. 97 - 102
Copyright
Copyright © Cambridge University Press 1978

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References

Barrett, J. & Beis, I. (1973). Studies on glycolysis in the muscle tissue of Ascaris lumbricoides (Nematoda). Comparative Biochemistry and Physiology 44B, 751–61.Google ScholarPubMed
Chong, C. & Taper, C. D. (1971). Daily variation of sorbitol and related carbohydrates in Malus leaves. Canadian Journal of Botany 49, 73–7.CrossRefGoogle Scholar
Christensen, H. N. & Palmer, G. A. (1967). Enzyme Kinetics. Philadelphia and London: W. B. Saunders Company.Google Scholar
Entner, N. (1957). The occurrence of the pentose phosphate pathway in Ascaris lumbricoides. Archives of Biochemistry and Biophysics 71, 52–61.CrossRefGoogle ScholarPubMed
Gabbay, K. H. (1972). Purification and immunological identification of bovine retinal aldose reductase. Israeli Journal of Medical Science 8, 1626–9.Google ScholarPubMed
Gabbay, K. H. (1973). The sorbitol pathway and the complications of diabetes. New England Journal of Medicine 288, 831–6.Google Scholar
Gabbay, K. H. & Cathcart, E. S. (1974). Purification and immunologic identification of aldose reductases. Diabetes 23, 460–8.CrossRefGoogle ScholarPubMed
Grossbard, L. & Schimke, R. T. (1966). Multiple hexokinases of rat tissues, purification and comparison of soluble forms. Journal of Biological Chemistry 241, 3546–60.Google Scholar
Harpur, R. P. (1963). Maintenance of Ascaris lumbricoides in vitro. II. Changes in muscle and ovary carbohydrates. Canadian Journal of Biochemistry and Physiology 41, 1673–89.CrossRefGoogle ScholarPubMed
Hers, H. G. (1960 a). L-aldoso-réductase. Biochimica et Biophysica Acta 37, 120–6.CrossRefGoogle Scholar
Hers, H. G. (1960 b). Le mécanisme de la formation du fructose séminal et du fructose foetal. Biochimica et Biophysica Acta 37, 127–38.CrossRefGoogle Scholar
King, T. E. & Mann, T. (1966). Sorbitol dehydrogenase from spermatozoa. In Methods in Enzymology, vol. 9 (ed. Wood, W. A.), pp. 159–63. New York and London: Academic Press.Google Scholar
Kockman, M. & Kwiatkowska, D. (1972). Purification and properties of fructose diphosphate aldolase from Ascaris suum muscle. Archives of Biochemistry and Biophysics 152, 856–68.CrossRefGoogle Scholar
Jedziniak, J. A. & Kinoshita, J. H. (1971). Activators and inhibitors of lens aldose reductase. Investigative Ophthalmology 10, 357–66.Google ScholarPubMed
Layne, E. (1957). Spectrophotometric and turbidometric methods for measuring proteins. In Methods in Enzymology, vol. 3 (ed. Colowick, S. P. and Kaplan, N. O.), p. 454. New York and London: Academic Press.Google Scholar
Nordlie, R. C. (1976). Glucose-6-phosphatase-phosphotransferase: relation to gluconeogenesis. In Gluconeogenesis: its Regulation in Mammalian Species, (ed. Hanson, R. W. and Mehlman, M. A.). New York and London; Sydney and Toronto: John Wiley and Son.Google Scholar
Rosenbluth, J. (1965). Ultrastructure of somatic muscle cells in Ascaris lumbricoides. II. Intermuscular junctions, neuromuscular junctions, and glycogen stores. Journal of Cell Biology 26, 579–91.CrossRefGoogle ScholarPubMed
Saz, H. J. & Lesoure, O. L. (1969). The functions of phosphoenolpyruvate carboxykinase and malic enzyme in the anaerobic formation of succinate by Ascaris lumbricoides. Comparative Biochemistry and Physiology 30, 49–60.CrossRefGoogle ScholarPubMed
Supowit, S. C. & Harris, B. G. (1976). Ascaris suum hexokinase; purification and possible function in compartmentation of glucose-6-phosphate in muscle. Biochimica et Biophysica Acta 422, 48–59.Google Scholar
Von Brand, T. (1973). Biochemistry of Parasites. New York and London: Academic Press.Google Scholar
Zanobini, A. & Firenzuoli, A. M. (1974). Influence of dietary sorbitol on some enzymes linked to glucose metabolism. Pharmacological Research Communications 6, 329–33.CrossRefGoogle ScholarPubMed