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Lysosomal enzymes and vitamin E deficiency

2. Gestation–resorption in the rat

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. Activities of β-glucuronidase, β-galactosidase, acid phosphatase and cathepsin were measured in the uterine contents of normal rats during gestation and of vitamin E-deficient rats during foetal resorption.

2. β-Glucuronidase activity reached a peak value on days 11 and 12, falling to lower values by day 14. Deficient rats showed slightly greater mean values than normal rats on days 11 and 12, but not after that time.

3. Vitamin E deficiency did not affect the activities of β-galactosidase, acid phosphatase and cathepsin, all of which showed a slow decrease during pregnancy.

4. The supernatant fraction of homogenates of uterine contents from deficient rats showed increased β-glucuronidase and β-galactosidase activity from day 14 to 17, suggesting some degree of rupture of the lysosomal membrane.

5. β-Glucuronidase and acid phosphatase activities were raised in the uteruses of some deficient rats towards the end of pregnancy, but serum β-glucuronidase was unaffected.

6. Changes in lysosomal hydrolases were not so marked during gestation–resorption as in some other vitamin E deficiency states, such as muscular dystrophy in the chick and rabbit.

Type
Research Article
Information
British Journal of Nutrition , Volume 21 , Issue 1 , February 1967 , pp. 137 - 145
Copyright
Copyright © The Nutrition Society 1967

References

Arata, L., Santoro, R., Severi, M. A. & Pecora, P. (1962). Boll. Soc. ital. Biol. sper. 38, 215.Google Scholar
Bloch, S. (1964). Acta anat. 56, 103.CrossRefGoogle Scholar
Bulmer, D. (1962). Nature, Lond. 195, 805.CrossRefGoogle Scholar
Bunyan, J., Green, J., Diplock, A. T. & Robinson, D. (1967). Br. J. Nutr. 21, 127.CrossRefGoogle Scholar
Cheng, D. W. & Thomas, B. H. (1953). Proc. Iowa Acad. Sci. 60, 290.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.CrossRefGoogle Scholar
Evans, H. M. & Burr, G. O. (1927). Mem. Univ. Calif. 8, 1.Google Scholar
Evans, H. M. & Bishop, K. S. (1922). Science, N.Y. 56, 650.CrossRefGoogle Scholar
Mason, K. E. & Harris, P. L. (1947). Biol. Symp. 12, 459.Google Scholar
Mora, J., Cañedo, L. & Soberön, G. (1965). Biochim. biophys. Acta 101, 137.CrossRefGoogle Scholar
Schaub, M. C. (1964). Experientia 20, 675.CrossRefGoogle Scholar
Woessner, J. F. (1965). Biochem. J. 97, 855.CrossRefGoogle 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