Hostname: page-component-77c89778f8-cnmwb Total loading time: 0 Render date: 2024-07-21T06:37:56.479Z Has data issue: false hasContentIssue false
  • English
  • Français

Metabolite levels and enzyme activities in the bovine mammary gland in different stages of lactation: II. Some metabolite levels and enzyme activities of the citric acid cycle

Published online by Cambridge University Press:  01 June 2009

Marianne Waldschmidt  and
S. Rilling
Marianne Waldschmidt
Affiliation:
Institute of Physiology, Technical University of Munich, 805 Freising-Weihenstephan, Germany
S. Rilling
Affiliation:
Institute of Physiology, Technical University of Munich, 805 Freising-Weihenstephan, Germany
Get access Rights & Permissions [Opens in a new window]

Summary

Samples of the mammary gland were obtained by the freeze-clamping technique from heifers, lactating and dry cows. Levels of acetyl CoA, citrate, isocitrate and α-oxoglutarate were determined in extracts of the samples and calculated per g fresh gland and per mg DNA. All mammary metabolite levels were significantly higher in lactating cows than in heifers or dry cows. The accumulation in the lactating gland increased in the sequence acetyl CoA–α-oxoglutarate–isocitrate–citrate. NADP/NADPH ratios in cytoplasm, as calculated from the equilibrium of isocitrate dehydrogenase, were lowest in lactating glands. The activities of some enzymes were also determined in the cytoplasm and calculated per g fresh gland, per mg protein and per mg DNA. Mammary citrate synthase activity did not vary significantly between different groups of cattle, whereas mammary isocitrate dehydrogenase activity was higher in lactating cows than in heifers or dry cows. No activity of ATP citrate lyase was detected.

Type
Research Article
Information
Journal of Dairy Research , Volume 40 , Issue 3 , October 1973 , pp. 361 - 370
Copyright
Copyright © Proprietors of Journal of Dairy Research 1973

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. & Cheng, W. (1969). Journal of Dairy Science 52, 523.CrossRefGoogle Scholar
Baldwin, R. L., Lin, H. J., Cheng, W., Cabrera, R. & Ronning, M. (1969). Journal of Dairy Science 52, 183.CrossRefGoogle Scholar
Baldwin, R. L. & Milligan, L. P. (1966). Journal of Biological Chemistry 241, 2058.CrossRefGoogle Scholar
Bauman, D. E., Brown, R. E. & Davis, C. L. (1970). Archives of Biochemistry and Biophysics 140, 237.CrossRefGoogle Scholar
Bergmeyer, H. U. (1970). Methoden der enzymatischen Analyse. Weinheim/Bergstrasse: Verlag Chemie, pp. 1532 ff.Google Scholar
Buckel, W. & Eggerer, H. (1965). Biochemische Zeitschrift 343, 29.Google Scholar
Cleland, W. W., Thompson, V. W. & Barden, R. E. (1969). Methods in Enzymology 13, 30.CrossRefGoogle Scholar
Gruber, W. & Moellering, H. (1966). Biochemische Zeitschrift 346, 85.Google Scholar
Gumaa, K. A., Greenbaum, A. L. & McLean, P. (1971). Proceedings of the Easter School in Agricultural Science, University of Nottingham 1970, 17, 197. (Lactation, ed. Falconer, I. R..)Google Scholar
Hardwick, D. C. (1965). Biochemical Journal 95, 233.CrossRefGoogle Scholar
Hardwick, D. C., Linzell, J. L. & Mepham, T. B. (1963). Biochemical Journal 88, 213.CrossRefGoogle Scholar
Srere, P. A., Brazil, H. & Gonen, L. (1963). Acta chemica Scandinavica 17, Supplement no. 1, S129.CrossRefGoogle Scholar
Takeda, Y., Suzuki, F. & Inoue, H. (1969). Methods in Enzymology 13, 153.CrossRefGoogle Scholar
Veech, R. L., Eggleston, L. V. & Krebs, H. A. (1969). Biochemical Journal 115, 609.CrossRefGoogle Scholar
Waldschmidt, M. (1973). Journal of Dairy Research 40, 7.CrossRefGoogle Scholar