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The differential effect of magnesium deficiency on isoenzymes of alkaline phosphatase (EC 3.1.3.1) in rat tissues

Published online by Cambridge University Press:  09 March 2007

M. F. Nehlawi
Affiliation:
Department of Biological Sciences, University of Lancaster, LancasterLA1 4YQ
F. W. Heaton
Affiliation:
Department of Biological Sciences, University of Lancaster, LancasterLA1 4YQ
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Abstract

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1. Alkaline phosphatase (EC 3.1.3.1) from many rat tissues was separated into two or three bands by electrophoresis on polyacrylamide gel. Ten of the bands had different electrophoretic mobilities, but some were present in more than one tissue.

2. Bands from the corresponding tissues of magnesium-deficient and control rats were qualitatively similar, but there were quantitative differences in the distribution of enzyme activity between them.

3. Mg deficiency had differential effects on the absolute activity of individual bands, but two main types of response were observed. There was an increase in the activity of the first bands from liver and kidney, the second band from femur and both bands from spleen, whereas the first band from femur, the first and second bands from intestinal mucosa and the second bands of serum, liver and kidney all decreased in activity during the deficiency.

4. The change in total alkaline phosphatase activity of a tissue during Mg deficiency depended on the ratio between the enzyme components within it.

Type
Papers on General Nutrition
Copyright
Copyright © The Nutrition Society 1979

References

Bessey, O. A., Lowry, O. H. & Brock, M. J. (1946). J. biol. Chem. 164, 321.CrossRefGoogle Scholar
Bussell, N. E., Vogel, J. J. & Levy, B. M. (1974). Proc. Soc. exp. Biol. Med. 145, 574.Google Scholar
Butterworth, P. J. & Moss, D. W. (1966). Nature, Lond. 209, 805.Google Scholar
Colbeau, A. & Maroux, S. (1978). Biochim. biophys. Acta 511, 39CrossRefGoogle Scholar
Conyers, B. A. J., Birkett, D. J., Neale, F. C., Posen, S. & Brudenell-Woods, J. (1967). Biochim. biophys. Acta 139, 363.CrossRefGoogle Scholar
Eaton, R. H. & Moss, D. W. (1967). Biochem. J. 105, 1307.Google Scholar
Fernley, H. N. & Walker, P. G. (1967). Biochem, J. 104, 1011.CrossRefGoogle Scholar
Fräki, J., Ruuskanen, O. & Kouvalainen, K. (1977). Biochim. biophys. Acta 482, 370.Google Scholar
Hamuro, Y. (1971). J. Nutr. 101, 635.CrossRefGoogle Scholar
Heaton, F. W. (1965). Nature, Lond. 207, 1292.CrossRefGoogle Scholar
Heaton, F. W. & Anderson, C. K. (1965). Clin Sci. 28, 99.Google Scholar
Langman, M. J. S., Constantinopoulos, A. & Bouchier, I. A. D. (1968). Nature, Lond. 217, 863.CrossRefGoogle Scholar
Larvor, P., Girard, A., Brochart, M., Parodi, A. & Sevestre, J. (1964). Annls Biol. anim. Biochim. Biophys. 4, 345.CrossRefGoogle 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.CrossRefGoogle Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). J. biol. Chem. 193, 265.CrossRefGoogle Scholar
Malik, N. & Butterworth, P. J. (1976). Biochem. Soc. Trans. 4, 646.Google Scholar
Markert, C. L. & Whitt, G. S. (1968). Experientia 24, 977.Google Scholar
Melani, F. & Farnararo, M. (1969). Biochim. biophys. Acta 178, 93.Google Scholar
Morton, R. K. (1953). Biochem. J. 55, 786.Google Scholar
Nayudu, P. R. V. & Hercus, F. B. (1974). Biochem. J. 141, 93.CrossRefGoogle Scholar
Neafsey, P. J. & Schwartz, R. (1977). J. Nurr. 107, 1061.Google Scholar
Nehlawi, M. F. (1976). The effects of magnesium deficiency on isoenzymes of alkaline phosphatase in rat tissues. MSc Thesis, University of Lancaster.Google Scholar
Nehlawi, M. F. & Heaton, F. W. (1978). Clinica chim. Acta 88, 577.Google Scholar
Ramadoss, C. S., Selvam, R., Shanmugasundaram, K. R. & Shanmugasundararn, E. R. B. (1977). J. Biochem., Tokyo 81, 1813.Google Scholar
Saini, P. K. & Done, J. (1972). Biochim. biophys. Acta 258, 147.CrossRefGoogle Scholar
Yokota, Y. (1978). J. Biochem., Tokyo 83, 1285.CrossRefGoogle Scholar
Young, J. M. (1967). J. clin. Purh. 20, 647.Google Scholar