Hostname: page-component-76fb5796d-zzh7m Total loading time: 0 Render date: 2024-04-29T18:44:59.290Z Has data issue: false hasContentIssue false

Blood pyruvate carboxylase (EC 6.4.1.1) activity as a criterion of biotin status in chickens and turkeys

Published online by Cambridge University Press:  26 April 2012

C. C. Whitehead
Affiliation:
Agricultural Research Council's Poultry Research Centre, King's Buildings, West Mains Road, Edinburgh EH9 3JS
D. W. Bannister
Affiliation:
Agricultural Research Council's Poultry Research Centre, King's Buildings, West Mains Road, Edinburgh EH9 3JS
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. Blood pyruvate carboxylase (pyruvate-CO2 ligase (ADP-forming); EC 6.4.1.1; PC) activities in young chickens and turkeys given low-biotin diets supplemented with biotin at graded levels were studied in three experiments.

2. In both species PC activity was related positively to the supplemental biotin level. The relationship was sigmoid and maximum activity was attained with supplemental levels above those required to give maximal growth response.

3. Enzyme activity decreased between 2 and 4 weeks of age but remained almost constant thereafter.

4. Activity in chicks was not affected by alterations in the fat or protein content of the diet.

5. Changing poults from high to low and from low to high supplemental biotin levels resulted in reversals in the levels of enzyme activity.

6. It is concluded that blood PC activity is a promising new criterion for assessing the biotin status of young chickens and turkeys.

Type
Papers on General Nutrition
Copyright
Copyright © The Nutrition Society 1978

References

REFERENCES

Achuta Murthy, P. N. & Mistry, S. P. (1972). J. scient. ind. Res. 31, 554.Google Scholar
Anderson, J. O. & Warnick, R. E. (1970). Poult. Sci. 49, 569.CrossRefGoogle Scholar
Atwal, A. S., Robblee, A. R. & Milligan, L. P. (1971). J. Nutr. 101, 1555.CrossRefGoogle Scholar
Bannister, D. W. & Whitehead, C. C. (1976). Int. J. Biochem. 7, 619.CrossRefGoogle Scholar
Brin, M., Tai, M., Ostashever, A. S. & Kalinsky, H. (1960). J. Nutr. 71, 273.CrossRefGoogle Scholar
Dakshinamurti, K., Landman, A. D., Ramamurti, L. & Constable, R. J. (1974). Analyt. Biochem. 61, 225.CrossRefGoogle Scholar
Frigg, M. (1976). Poult. Sci. 55, 2310.CrossRefGoogle Scholar
Frigg, M., Weiser, H. & Bollinger, A. (1973). 5th int. Congr. Wld Vet. Poult. Ass., Munich, 2, 1286.Google Scholar
Glatzle, D. & Frigg, M. (1975). Biochem. biophys. Res. Commun. 66, 368.CrossRefGoogle Scholar
Glatzle, D., Weber, F. & Wiss, O. (1968). Experientia, 24, 1122.CrossRefGoogle Scholar
Hood, R. L. (1975). J. Sci. Fd Agric. 26, 1847.CrossRefGoogle Scholar
Hood, R. L., Johnson, A. R., Fogerty, A. C. & Pearson, J. A. (1976). Aust. J. biol Sci. 29, 429.CrossRefGoogle Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). J. biol. Chem. 193, 265.CrossRefGoogle Scholar
Moss, J. & Lane, M. D. (1971). Adv. Enzymol. 35, 321.Google Scholar
Whitehead, C. C. (1977). Wld's Poult Sci. J. 33, 140.CrossRefGoogle Scholar
Whitehead, C. C., Bannister, D. W. & Cleland, M. E. (1978). Br. J. Nutr. (in the Press).Google Scholar
Wright, L. D. & Skeggs, H. R. (1944). Proc. Soc. exp. Biol. Med. 56, 95.CrossRefGoogle Scholar