Hostname: page-component-586b7cd67f-gb8f7 Total loading time: 0 Render date: 2024-11-24T00:34:48.620Z Has data issue: false hasContentIssue false
  • English
  • Français

Lysosomal enzymes and vitamin E deficiency

3. Liver necrosis and testicular degeneration 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, W 8
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. The activities of several lysosomal hydrolases have been measured in tissues of rats with nutritional liver necrosis. Incipient or actual liver necrosis did not alter total, free or unsedimentable activities of cathepsin, β-glucuronidase, β-galactosidase or acid phosphatase of liver and kidney. Free hydrolytic activity towards p-nitrophenyl phosphate was slightly raised in liver, and serum β-galactosidase and β-glucuronidase were moderately elevated. These results suggest that lysosomal hydrolases are not directly implicated in the causation of liver necrosis.

2. Testicular degeneration was studied with reference to changes in β-giucuronidase activity. This enzyme activity, total, free and unsedimentable, was raised in deficient rat testis at 6 months old and did not decline even after a year. Raised values were also found in serum.

Type
Research Article
Information
British Journal of Nutrition , Volume 21 , Issue 1 , February 1967 , pp. 147 - 154
Copyright
Copyright © The Nutrition Society 1967

References

Arata, L. & Pecora, P. (1962). Boll. Soc. ital. Biol. sper. 38, 209.Google Scholar
Arata, L., Santoro, R., Severi, M. A. & Pecora, P. (1962 a). Boll. Soc. ital. Biol. sper. 38, 212.Google Scholar
Arata, L., Santoro, R., Severi, M. A. & Pecora, P. (1962 b). Boll. Soc. ital. Biol. sper. 38, 215.Google Scholar
Beaufay, H., van Campenhout, E. & de Duve, C. (1959). Biochem. J. 73, 617.CrossRefGoogle Scholar
Bieri, J. G., Dam, H., Prange, I. & Søndergaard, E. (1961). Acta physiol. Scand. 52, 36.CrossRefGoogle Scholar
Bunyan, J., Diplock, A. T., Edwin, E. E. & Green, J. (1962). Br. J. Nutr. 16, 519.CrossRefGoogle Scholar
Bunyan, J., Green, J., & Diplock, A. T. (1963). Br. J. Nutr. 17, 117.CrossRefGoogle Scholar
Bunyan, J., Green, J., Diplock, A. T. & Robinson, D. (1967 a), Br. J. Nutr. 21, 127.CrossRefGoogle Scholar
Bunyan, J., Green, J., Diplock, A. T. & Robinson, D. (1967 b). Br. J. Nutr. 21, 137.CrossRefGoogle Scholar
Bunyan, J., McHale, D. & Green, J. (1963). Br. J. Nutr. 17, 391.CrossRefGoogle Scholar
Corwin, L. M. (1962). Archs Biochem. Biophys. 97, 51.CrossRefGoogle Scholar
de Duve, C. & Beaufay, H. (1959). Biochem. J. 73, 610.CrossRefGoogle Scholar
Desai, I. D., Calvert, C. C. & Scott, M. L. (1964). Archs Biochem. Biophys. 108, 60.CrossRefGoogle Scholar
Dingle, J. T., Sharman, I. M. & Moore, T. (1966). Biochem. J. 98, 476.CrossRefGoogle Scholar
Evans, H. M. & Bishop, K. S. (1922), Science, N.Y. 56, 650.CrossRefGoogle Scholar
Furth, A. J. & Robinson, D. (1965). Biochem. J. 97, 59.CrossRefGoogle Scholar
Green, J., Edwin, E. E., Bunyan, J. & Diplock, A. T. (1960). Biochem. J. 75, 456.CrossRefGoogle Scholar
Harris, P. L. & Mason, K. E. (1956). Int. Congr. Vitam. E. III. Venice, 1955, p. 1.Google Scholar
Herraiz, M. L. & Radice, J. C. (1949). Ann. N.Y.Acad. Sci. 52, 88.Google Scholar
Himsworth, H. P. (1947). In Lectures on the Liver and its Diseases, p. 19. Oxford: Blackwell Scientific Publications.Google Scholar
Koszalka, T. R., Mason, K. E. & Krol, G. (1961). J. Nutr. 73, 78.CrossRefGoogle Scholar
Mattill, H. A. & Stone, N. C. (1923). J. biol. Chem. 55, 443.CrossRefGoogle Scholar
Nagel, W. & Willig, F. (1964). Nature, Lond. 201, 617.CrossRefGoogle Scholar
Neil, M. W. & Horner, M. W. (1964). Biochem. J. 92, 217.CrossRefGoogle Scholar
Piccardo, M. G. & Schwarz, K. (1958). In Liver Function, p. 528. [Brauer, R. W., editor.] Washington, D.C.: American Institute of Biological Sciences.Google Scholar
Schwarz, K. (1954). Ann. N.Y. Acad. Sci. 57, 878.CrossRefGoogle Scholar
Schwarz, K. (1958). In Liver Function, p. 509. [Brauer, R. W., editor.] Washington, D.C.: American Institute of Biological Sciences.Google Scholar
Schwarz, K. (1961). Am. J. clin. Nutr. 9, no. 4, part 2, p. 94.CrossRefGoogle Scholar
Schwarz, K. (1965). Fedn Proc. Fedn Am. Socs exp. Biol. 24, 58.Google Scholar
Schwarz, K., Bieri, J. G., Briggs, G. M. & Scott, M. L. (1957). Proc. Soc. exp. Biol. Med. 95, 621.CrossRefGoogle Scholar
Schwarz, K. & Foltz, C. M. (1957). J. Am. chem. Soc. 79, 3292.CrossRefGoogle Scholar
Schwarz, K. & Mertz, W. (1959). Metabolism 8, 79.Google Scholar
Trump, B. F., Goldblatt, P. J. & Stowell, R. E. (1962). Lab. Invest. 11, 986.Google Scholar
Warburg, O. & Christian, W. (1941). Biochem. Z. 310, 382.Google Scholar
Weissmann, G., Uhr, J. W., & Thomas, L. (1963). Proc. Soc.exp. Biol. Med. 112, 284.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