Hostname: page-component-54dcc4c588-5q6g5 Total loading time: 0 Render date: 2025-10-06T00:20:28.045Z Has data issue: false hasContentIssue false
  • English
  • Français

Transaminase activity in the rumen liquor of sheep

Published online by Cambridge University Press:  09 March 2007

Abdur Rekib  and
D. P. Sadhu
Abdur Rekib
Affiliation:
Indian Veterinary Research Institute, Izatnagar, UP, India
D. P. Sadhu
Affiliation:
Indian Veterinary Research Institute, Izatnagar, UP, India
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 presence of transaminase activity in rumen contents has been demonstrated. The level of activity varied with time after feeding and was influenced by the nature of the diet.

2. Rumen contents from a sheep given a diet containing casein showed greater transaminase activity at 2 h than at 6 h after feeding. Conversely, with a diet containing urea and maize, the activity was higher at 6 h than at 2 h after feeding.

3. The greater part of the transaminase activity of rumen liquor was associated with the fraction containing protozoa and food residues while the cell-free fraction contained no transaminase activity under the experimental conditions.

Information

Type
Research Article
Information
British Journal of Nutrition , Volume 22 , Issue 3 , September 1968 , pp. 325 - 329
Copyright
Copyright © The Nutrition Society 1968

References

Akkada, A. R. A. & Howard, B. H. (1962). Biochem. J. 82, 313.CrossRefGoogle Scholar
Annison, E. F. (1956). Biochem. J. 64, 705.CrossRefGoogle Scholar
Annison, E. F. & Lewis, D. (1959). Metabolism in the Rumen, 1st ed. London: Methuen.Google Scholar
Appleby, J. C. (1955). J. gen. Microbiol. 12, 526.CrossRefGoogle Scholar
Blackburn, T. H. & Hobson, P. N. (1960). J. gen. Microbiol. 22, 282.CrossRefGoogle Scholar
Blincoe, C. & Dye, W. B. (1958). J. Anim. Sci. 17, 224.CrossRefGoogle Scholar
Braunstein, A. E. & Kritzmann, M. G. (1937–1938). Enzymologia 2, 129.Google Scholar
Cammarata, P. S. & Cohen, P. P. (1950). J. biol. Chem. 187, 439.CrossRefGoogle Scholar
Feldman, L. I. & Gunsalus, I. C. (1950). J. biol. Chem. 187, 821.CrossRefGoogle Scholar
Hunt, W. G. & Moore, R. O. (1958). Appl. Microbiol. 6, 36.CrossRefGoogle Scholar
McDonald, I. W. (1954). Biochem. J. 56, 120.CrossRefGoogle Scholar
Meister, A. & Tice, S. V. (1950). J. biol. Chem. 187, 173.CrossRefGoogle Scholar
Otagaki, K. K., Black, A. L., Goss, H. & Kleiber, M. (1955). J. agric. Fd Chem. 3, 948.CrossRefGoogle Scholar
Sall, T., Richards, H. K., Harrison, E. & Myerson, R. M. (1957). J. Lab. clin. Med. 50, 297.Google Scholar