Hostname: page-component-586b7cd67f-dsjbd Total loading time: 0 Render date: 2024-11-23T21:08:39.273Z Has data issue: false hasContentIssue false

The effect of zinc deficiency on alkaline phosphatase (EC 3.1.3.1) and its isoenzymes

Published online by Cambridge University Press:  09 March 2007

F. A. Adeniyi
Affiliation:
Department of Biological Sciences, University of Lancaster, Lancaster LA 1 4YQ
F. W. Heaton
Affiliation:
Department of Biological Sciences, University of Lancaster, Lancaster LA 1 4YQ
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. Zinc deficiency in young rats reduced both the total alkaline phosphatase (EC 3.1.3.1) activity and Zn concentration in serum, kidney, small intestine and femur.

2. Addition of 0.01 mM-exogenous Zn had no greater activating effect with extracts of kidney, small intestine and femur from Zn-deficient than control rats, indicating that the main effect of the deficiency was on the amount of enzyme present rather than the efficiency of its operation. Exogenous Zn increased the activity of enzyme in serum of Zn-deficient rats, but it was still lower than in the serum of control animals.

3. Electrophoresis on polyacrylamide gel separated the alkaline phosphatase activity from all tissues into two bands. The bands had similar electrophoretic mobilities and appeared to be qualitatively identical in corresponding tissues from Zn-deficient and control rats.

4. Zn deficiency eliminated the first band found in serum from control rats and it had selective effects on the activity of individual bands in other tissues. The major inhibitory effect was on the first bands of enzyme activity in kidney and femur, but in small intestine only the second band was affected. In liver the activity of the first band was increased and that of the second band decreased by similar amounts.

Type
Papers on General Nutrition
Copyright
Copyright © The Nutrition Society 1980

References

REFERENCES

Adeniyi, F. A. & Heaton, F. W. ( 1979). IRCS Med. Sci. 7, 145.Google Scholar
Alfaro, B. & Heaton, F. W. ( 1973). Br. J. Nutr. 29, 73..Google Scholar
Cathala, G., Brunel, C., Chappelet-Tordo, D. & Lazdunski, M. ( 1975). J. biol. Chem. 250, 6046..Google Scholar
Conyers, R. A. J., Birkett, D. J., Neale, F. C., Posen, S. & Brudenell-Woods, J. ( 1967). Biochirn. biophys. Acta 139, 363.Google Scholar
Chesters, J. K. & Will, M. ( 1978). Er. J. Nutr. 39, 297..Google Scholar
Gubler, C. J.,Lahey, M. E., Ashenbrucker, H., Cartwight, G. E. & Wintrobe, M. M. ( 1952). J. biol. Chem. 196, 209.Google Scholar
Huber, A. M. & Gershoff, S. N. ( 1973). J. Nutr. 103, 1175.Google Scholar
Kfoury, G. A., Reinhold, J. G. & Simonian, S. ( 1968). J. Nutr. 95, 102.Google Scholar
Linden, G., Chappelet-Tordo, D. & Lazdunski, M. ( 1977). Biochim. biophys. Acta 483, 100.Google Scholar
Loveless, B. W. & Heaton, F. W. ( 1976). Br. J. Nutr. 36, 487..Google Scholar
Loveless, B. W., Williams, P. & Heaton, F. W. ( 1972). Br. J. Nutr. 28, 261.Google Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. ( 1951). J. biol. Chem. 193, 265..Google Scholar
Luecke, R. W., Olman, M. E. & Baltzer, B. V. ( 1968). J. Nutr. 94, 344..Google Scholar
Morton, R. K. ( 1953). Biochem. J. 55, 786..Google Scholar
Nehlawi, M. F. & Heaton, F. W. ( 1979). Br. J. Nutr. 42, 105..CrossRefGoogle Scholar
Prasad, A. S., Oberleas, P., Wolf, P. & Horwitz, J. P. ( 1967). J. clin. Invest. 46, 549..CrossRefGoogle Scholar
Ramadoss, C. S., Selvam, R., Shanmugasundarum, K. R. & Shanmugasundaram, E. R. B. ( 1977). J. Biochem., Tokyo 81, 1813.Google Scholar
Saini, P. K. & Done, J. ( 1972). Biochim. biophys. Acta 258, 147.CrossRefGoogle Scholar
Wooton, I. D. P. ( 1964). Microanalysis in Medical Biochemistry, 4th ed., p. 101. London: J. &A. Churchill.Google Scholar
Yokota, Y. ( 1978). J. Biochem., Tokyo 83, 1285.CrossRefGoogle Scholar