Hostname: page-component-cd9895bd7-7cvxr Total loading time: 0 Render date: 2024-12-25T02:41:58.941Z Has data issue: false hasContentIssue false
  • English
  • Français

Changes in plasma concentrations of thyroxine binding prealbumin and retinol binding protein in Japanese quail after hatching

Published online by Cambridge University Press:  09 March 2007

D. J. Heaf ,
M. El-Sayed  and
J. Glover
D. J. Heaf
Affiliation:
Department of Biochemistry, University of Liverpool, P.O. Box 147, Liverpool, L69 3BX
M. El-Sayed
Affiliation:
Department of Biochemistry, University of Liverpool, P.O. Box 147, Liverpool, L69 3BX
J. Glover
Affiliation:
Department of Biochemistry, University of Liverpool, P.O. Box 147, Liverpool, L69 3BX
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. Male and female Japanese quail (Coturnix coturnix japonica) were reared under short daily photoperiods (8 h light–16 h dark) to inhibit sexual development with free access to food and water. Blood was sampled at frequent intervals for 13 weeks from hatching in order to monitor the developmental changes in plasma concentrations of the two proteins which are important in the transport of retinol, retinol-binding protein (RBP) and thyroxine-binding prealbumin (TBPA).

2. Measurements of body-weight, blood packed cell volume and plasma total protein concentration showed that the birds had a normal pattern of growth and haematological development. Plasma concentrations of TBPA, total immunoreactive RBP (IRBP) and holoRBP were 220, 60 and 45 μg/ml respectively in 1-d-old quail and rose to 430, 165 and 140 μg/ml at 14 d of age, which was 10 d after the corresponding change in total protein. Neither RBP nor TBPA concentrations were significantly different between the sexes during the 13 weeks, but there were minor fluctuations in concentration within relatively narrow limits.

Type
Papers on General Nutrition
Information
British Journal of Nutrition , Volume 44 , Issue 3 , November 1980 , pp. 287 - 293
Copyright
Copyright © The Nutrition Society 1980

References

REFERENCES

Abe, T., Muto, Y. & Hosoya, N. (1976). Life Sci. 17, 1579.CrossRefGoogle Scholar
Atwal, O. S., Mcfarland, L. Z. & Wilson, W. O. (1964). Poultry Sci. 4, 1392.Google Scholar
El-Sayed, M., Heaf, D. J. & Glover, J. (1980). Gen. Comp. Endocrinol. 41.Google Scholar
Gitlin, D. & Gitlin, J. D. (1975). In The Plasm Proteins. Structure Function and Genetic Control, 2nd ed. vol. 2, p. 264 [Putnam, F. W, editor]. New York: Academic Press.Google Scholar
Glover, J., Heaf, D. J. & Large, S. (1980). Br. J. Nutr. 43, 357.Google Scholar
Glover, J., Jay, C., Kershaw, R. C. & Reilly, P. E. B. (1976). Br. J. Nutr. 36, 137.Google Scholar
Glover, J. & Large, S. (1977). Proc. Nutr. Soc. 36, 85A.Google Scholar
Glover, J., Moxley, L., Muhilal, H. & Weston, S. (1974). Clinica chim. Acta 50, 371.Google Scholar
Griminger, P. (1976). In Avian Physiology, 3rd ed. p. 233 [Sturkie, P. D., editor]. New York: Springer-Verlag.CrossRefGoogle Scholar
Heaf, D. J. & Glover, J. (1979). J. Endocr. 83, 475.CrossRefGoogle Scholar
Heaf, D. J., Pythian, B., El-Sayed, M. & Glover, J. (1980). Int. J. Biochem. (In the Press.)Google Scholar
Heller, J. (1976). Devel. Biol. 51, I.CrossRefGoogle Scholar
Ingenbleek, Y. (1977). La malnutrition proteino-calorique chez l'enfant en bas age, repercussions Sur la fonction thyroidienne et les proteines vectrices du serum. Thesis, University of Dakar.Google Scholar
Jacobsen, B. B., Peiterson, B.. Andersen, H. J. & Hummer, L. (1979). Acta Paediat. scand. 68, 49.Google Scholar
Kanai, M., Raz, A. & Goodman, D. S. (1968). J. clin. Invest. 47, 2025.CrossRefGoogle Scholar
Kershaw, R. C. (1978). Factors controlling plasma retinol-binding protein. PhD Thesis, University of Liverpool.Google Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). J. biol. Chem. 193, 265.CrossRefGoogle Scholar
Mancini, G., Carbonara, A. O. & Heremans, J. F. (1965). Immunochemistry 2, 235.Google Scholar
Muhilal, H. & Glover, J. (1974). Br. J. Nutr. 32, 549.CrossRefGoogle Scholar
Muto, Y., Smith, J. E., Milch, P. O. & Goodman, D. S. (1972). J. biol. Chem. 247, 2542.CrossRefGoogle Scholar
Nirmalan, G. P. & Robinson, G. A. (1971). Br. Poult. Sci. 12, 475.CrossRefGoogle Scholar
Smith, F. R., Raz, A. & Goodman, D. S. (1970). J. chi. Invest. 49. 1754.Google Scholar
Sreekrishna, K. & Cam, H. R. (1978). Indian J. Eiochem. Eiophys. 15, 255.Google Scholar
Sturkie, P. D. (1976). In Avian Physiology, 3rd ed., p. 54 [Sturkie, P. D., editor]. New York: Springer-Verlag.CrossRefGoogle Scholar
Takahashi, Y. I., Smith, J. E. & Goodman, D. S. (1977). Am. J. Physiol. 233, 263.Google Scholar
Tata, J. R. & Shellabarger, C. J. (1959). Biochem. J. 72, 608.CrossRefGoogle Scholar
Thompson, J. N. (1970). In Fat Soluble Vitamins, p. 267 [De Luca, J. F. and Suttie, J.W., editors]. Madison: University of Wisconsin Press.Google Scholar
Thompson, J. N., Howell, J. McC. & Pitt, G. A. J. (1964). Proc. R. Soc. B 159, 510.Google Scholar
Thompson, J. N., Howell, J. McC., Pitt, G. A. J. & McLaughlin, C. (1969). Br. J. Nutr. 23. 471.Google Scholar
Vahlquist, A., Rask, L., Peterson, P. A. & Berg, T. (1975). Scand. J. clin. Lab. Invest. 35, 569.Google Scholar
Woodard, A. E., Abpanalp, H., Wilson, W. O. & Vohm, P. (1973). In Japanese Quail Husbandry in the Luboratory, p. 22. Department of Avian Sciences, University of California.Google Scholar