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Lysosomal enzymes and vitamin E deficiency

1. Muscular dystrophy, encephalomalacia and exudative diathesis in the chick

Published online by Cambridge University Press:  09 March 2007

J. Bunyan ,
J. Green ,
A. T. Diplock  and
D. Robinson
J. Bunyan
Affiliation:
Walton Oaks Experimental Station, Vitamins Ltd, Tadworth, Surrey
J. Green
Affiliation:
Walton Oaks Experimental Station, Vitamins Ltd, Tadworth, Surrey
A. T. Diplock
Affiliation:
Walton Oaks Experimental Station, Vitamins Ltd, Tadworth, Surrey
D. Robinson
Affiliation:
Department of Nutrition, Queen Elizabeth College, London, W8
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Abstract

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1. The activities of several lysosomal hydrolases were measured in the tissues of chicks suffering from nutritional muscular dystrophy, encephalomalacia or exudative diathesis.

2. In dystrophic breast muscle, β-glucuronidase was raised five- to six-fold, cathepsin fourfold and acid phosphatase 1.5-fold. No change was found in the subcellular distribution of β-glucuronidase.

3. Chicks with encephalomalacia showed no changes in the β-glucuronidase, β-galactosidase, acid phosphatase or β-acetylglucosaminase activities of cerebellum or brain. Subcellular distribution of β-glucuronidase and β-galactosidase in these tissues was also unchanged.

4. In exudative diathesis, hydrolases were found in the exudate, and there was increased activity in the subcutaneous tissue first showing haemorrhages. Increased hydrolytic activity was found in liver, spleen and kidney. Breast muscle was not always affected by the exudative condition, but, when it too degenerated, its hydrolase activity increased.

5. β-Glucuronidase activity was measured in the serums of chicks suffering from each of the three deficiency diseases. None of the diseases caused a rise in activity.

Type
Research Article
Information
British Journal of Nutrition , Volume 21 , Issue 1 , February 1967 , pp. 127 - 136
Copyright
Copyright © The Nutrition Society 1967

References

Borooah, J., Leaback, D. H. & Walker, P. G. (1957). Biochem. J. 65, 15p.Google Scholar
Bunyan, J., Diplock, A. T., Edwin, E. E. & Green, J. (1962). Br. J. Nutr. 16, 519.Google Scholar
de Duve, C. & Berthet, J. (1953). Nature, Lond. 172, 1142.CrossRefGoogle Scholar
de Duve, C., Pressman, B. C., Gianetto, R., Wattiaux, R. & Appelmans, F. (1955). Biochem. J. 60, 604.Google Scholar
Desai, I. D. (1966). Nature, Lond. 209, 1349.Google Scholar
Desai, I. D., Calvert, C. C. & Scott, M. L. (1964). Archs Biochem. Biophys. 108, 60.CrossRefGoogle Scholar
Desai, I. D., Calvert, C. C., Scott, M. L. & Tappel, A. L. (1964). Proc. Soc. exp. Biol. Med. 115, 462.Google Scholar
Findlay, J., Levvy, G. A. & Marsh, C. A. (1958). Biochem. J. 69, 467.Google Scholar
Gianetto, R. & de Duve, C. (1955). Biochem. J. 59, 433.CrossRefGoogle Scholar
Hurst, R. O. (1964). Can. J. Biochem. Physiol. 42, 287.Google Scholar
Jibril, A. O. & McCay, P. B. (1965). Nature, Lond. 205, 1214.Google Scholar
Kunitz, M. (1947). J. gen. Physiol. 30, 291.Google Scholar
Mead, J. A. R., Smith, J. N. & Williams, R. T. (1955). Biochem. J. 61, 569.Google Scholar
Robinson, D. (1957). Biochem. J. 67, 6P.Google Scholar
Robinson, D. (1964). Comp. Biochem. Physiol. 12, 95.Google Scholar
Scott, M. L. & Calvert, C. C. (1962). J. Nutr. 77, 105.CrossRefGoogle Scholar
Tappel, A. L., Sawant, P. L. & Shibko, S. (1963) In Ciba Foundn Symp: Lysosomes, p. 78. [de Reuck, A.V.S. and Cameron, M. P., editors.] London: J. and A. Churchill Ltd.CrossRefGoogle Scholar
Weinstock, I. M., Goldrich, A. D. & Milhorat, A. T. (1955). Proc. Soc. exp. Biol. Med. 88, 257.CrossRefGoogle Scholar
Weinstock, I. M., Goldrich, A. D. & Milhorat, A. T. (1956). Proc. Soc. exp. Bid. Med. 91, 302.Google Scholar
Zalkin, H., Tappel, A. L., Caldwell, K. A., Shibko, S., Desai, I. D. & Holliday, T. A. (1962). J. biol. Chem. 237, 2678.CrossRefGoogle Scholar