Hostname: page-component-78c5997874-m6dg7 Total loading time: 0 Render date: 2024-11-03T00:27:50.456Z Has data issue: false hasContentIssue false

The induction by exogenous hormones of enzymes metabolising glucose 6-phosphate in the mammary gland of the pseudopregnant rabbit

Published online by Cambridge University Press:  01 June 2009

R. J. Heitzman
Affiliation:
Institute for Research on Animal Diseases, Compton, Newbury, Berkshire

Summary

A study was made of the effects of the hormones, prolactin and cortisol acetate, on the activities in the mammary gland of the pseudopregnant rabbit of the enzymes concerned with lactose biosynthesis and glucose 6-phosphate metabolism, namely: UDP-glucose pyrophosphorylase, UDP-glucose-4'-epimerase, phosphofructokinase, phosphoglucomutase, glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Significant increases in enzyme activities were observed in rabbits examined 3 or 4 days after receiving a mammary intraductal injection of prolactin. The activities were not significantly increased at examination 2 days after injection of prolactin. Rabbits receiving cortisol acetate each day for 3 days also showed no significant increases in mammary enzyme activity. However, when prolactin and cortisol acetate were given simultaneously over a period of 3 days, increased enzyme activities were found suggesting synergistic action of the hormones.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1969

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Baldwin, R. L. (1966). J. Dairy Sci. 49, 1533.CrossRefGoogle Scholar
Barnawell, E. B. (1967). Endocrinology 80, 1083.CrossRefGoogle Scholar
Bradley, T. R. & Clarke, P. M. (1956). J. Endocr. 14, 28.CrossRefGoogle Scholar
Cowie, A. T. (1961). In Milk, the Mammary Gland and its Secretion, vol. I, p. 163 (Eds. Kon, S. K. and Cowie, A. T.). New York and London: Academic Press Inc.Google Scholar
Dische, Z. (1955). In The Nucleic Acids. 1st edn., vol. 1, p. 287. (Eds. Chargaff, E. and Davidson, J. N.). New York: Academic Press Inc.Google Scholar
Heitzman, R. J. (1967). Biochem. J. 104, 24P.Google Scholar
Heitzman, R. J. (1968a). J. Endocr. 40, 81.CrossRefGoogle Scholar
Heitzman, R. J. (1968b). J. Endocr. 41, xvi.Google Scholar
Jones, E. A. (1967). Biochem. J. 103, 420.CrossRefGoogle Scholar
Lockwood, D. H., Turkington, R. W. & Topper, Y. J. (1966). Biochim. biophys. Acta 130, 493.CrossRefGoogle Scholar
Meites, J., Hopkins, T. J. & Talwalker, P. K. (1963). Endocrinology 73, 261.CrossRefGoogle Scholar
Schneider, W. C. (1945). J. biol. Chem. 161, 293.CrossRefGoogle Scholar
Shatton, J. B., Gruenstein, M., Shay, H. & Weinhouse, S. (1965). J. biol. Chem. 240, 22.CrossRefGoogle Scholar
Thibodeau, P. S. & Thayer, S. A. (1967). Endocrinology 80, 505.CrossRefGoogle Scholar