Hostname: page-component-5c6d5d7d68-wpx84 Total loading time: 0 Render date: 2024-08-23T17:19:07.744Z Has data issue: false hasContentIssue false

Carnitine secretion into milk of ruminants

Published online by Cambridge University Press:  01 June 2009

A. M. Snoswell
Affiliation:
Department of Agricultural Biochemistry, Waite Agricultural Research Institute, University of Adelaide, Glen Osmond, South Australia 5064, Australia
J. L. Linzell
Affiliation:
Agricultural Research Council, Institute of Animal Physiology, Babraham, Cambridge, CB2 4AT

Summary

Total acid-soluble carnitine concentration in cow's, goat's and ewe's milk was 117, 101 and 872 nmol/ml respectively, of which acetylcarnitine made up 30% in goats, 10% in cows and 11% in ewes. The concentration of carnitine in the arterial blood of goats decreased significantly (P < 0·01) with the onset of lactation from 18·1 to 8·4nmol/ml and during lactation in goats and cows there was a significant arterio-venous difference of carnitine across the udder, with mean extractions of 14 and 5% respectively. Calculation of the udder uptake of carnitine, from these figures and from udder blood-flows, showed that in goats the amount lost in the milk was much less than that taken from the blood, but in cows about the same. Two groups of lactating ewes on low and high nutritional planes were sampled at 2-weekly intervals from 2 to 8 weeks of lactation. The concentrations of total acid-soluble carnitine and acetylcarnitine in the milk were similar in the 2 groups and remained relatively constant over this period, but the total acid-soluble carnitine concentration in jugular blood from the ewes on the low nutritional plane was significantly (P < 0·01) higher than from the ewes on the higher nutritional plane from the fourth week of lactation. The total acid-soluble carnitine concentration in liver of goats was 290 nmol/g wet wt; mammary gland, 324; kidney-cortex, 692; heart, 2030 and skeletal muscle, 14300. Carnitine acetyltransferase (E.C. 2.3.1.7) activity of mammary tissue from lactating ewes was 0·6 μmol per min per g wet wt of which approximately half appeared to be ‘latent’ or membrane bound. Acetate thiokinase (E.C. 6.2.1.1) activity in this tissue was found to be 1·5 μmol per min per g wet wt and was predominantly localized in the cytoplasm. Carnitine palmitoyltransferase (E.C. 2.3.1.21) activity in the same tissue was 0·8 μmol per min per g wet wt while no acetylcarnitine hydrolase activity could be detected. The results suggest that carnitine in mammary tissue is extracted from the blood for the oxidation of both acetate and long-chain fatty acids and that some is lost in the milk.

Type
Research Article
Copyright
Copyright © Proprietors of Journal of Dairy Research 1975

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

Annison, E. F. & Linzell, J. L. (1964). Journal of Physiology 175, 372.CrossRefGoogle Scholar
Barker, P. J., Fincham, N. J. & Hardwick, D. C. (1968). Biochemical Journal 110, 739.CrossRefGoogle Scholar
Bøhmer, T. (1974). Biochimica et Biophysica Acta 343, 551.CrossRefGoogle Scholar
Broekhuysen, J. & Deltour, G. (1961). Annales de Biologie Clinique 9, 549.Google Scholar
Brooks, D. E., Hamilton, D. W. & Mallek, A. H. (1973). Biochemical and Biophysical Research Communications 52, 1354.CrossRefGoogle Scholar
Brooks, D. E., Hamilton, D. W. & Mallek, A. H. (1974). Journal of Reproduction and Fertility 36, 141.CrossRefGoogle Scholar
Cederblad, G. & Lindstedt, S. (1972). Clinica Chimica Acta 37, 235.CrossRefGoogle Scholar
Costa, N. D. & Snoswell, A. M. (1974). Proceedings of the Australian Biochemical Society 7, 36.Google Scholar
Erfle, J. D., Fisher, L. J. & Sauer, F. (1970). Journal of Dairy Science 53, 486.CrossRefGoogle Scholar
Erfle, J. D., Sauer, F. D. & Fisher, L. J. (1974). Journal of Dairy Science 57, 671.CrossRefGoogle Scholar
Fleet, I. R. & Linzell, J. L. (1974). Journal of Physiology 242, 1P.Google Scholar
Fritz, I. B. (1963). Advances in Lipid Research 1, 285.CrossRefGoogle Scholar
Haigler, H. T. & Broquist, H. P. (1974). Biochemical and Biophysical Research Communications 56, 676.CrossRefGoogle Scholar
Linzell, J. L. (1966). Circulation Research 18, 745.CrossRefGoogle Scholar
Linzell, J. L. & Peaker, M. (1971 a). Journal of Physiology 216, 683.CrossRefGoogle Scholar
Linzell, J. L. & Peaker, M. (1971 b). Physiological Reviews 51, 564.CrossRefGoogle Scholar
Marquis, N. R. & Fritz, I. B. (1964). Journal of Lipid Research 5, 184.CrossRefGoogle Scholar
Pearson, D. J. & Tubbs, P. K. (1964). Nature 202, 91.CrossRefGoogle Scholar
Pearson, D. J. & Tubbs, P. K. (1967). Biochemical Journal 105, 953.CrossRefGoogle Scholar
Shepherd, D. & Garland, P. B. (1969). Biochemical Journal 114, 597.CrossRefGoogle Scholar
Snoswell, A. M. & Henderson, G. D. (1970). Biochemical Journal 119, 59.CrossRefGoogle Scholar
Snoswell, A. M. & Koundakjian, P. P. (1972). Biochemical Journal 127, 133.CrossRefGoogle Scholar
Snoswell, A. M. & McIntosh, G. H. (1974). Australian Journal of Biological Sciences 27, 645650.CrossRefGoogle Scholar
Stadtman, E. R. (1957). Methods in Enzymology 3, 931.CrossRefGoogle Scholar