Abstract
CONTROVERSY has centred around the nature of the active groups influencing the activity of alkaline phosphatases of higher animals1. In a recent communication2, I suggested on the basis of results obtained with the alkaline phosphatase of the fungus Penicillium chrysogenum, Q-176, that the activity of the enzyme is influenced by both zinc and magnesium ions and that the relative proportion in which these ions existed in an active state determined the pH of optimum activity.
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Cloetens, R., Biochem. Z., 308, 37 (1941) ; 310, 42 (1941) ; Arch. Int. Pharmacodyn., 68, 419 (1942). Hove, E., Elvehjem, C. A., and Hart, E. B., J. Biol. Chem., 134, 426 (1940). Thoai, N. v., Roche, J., and Roger, M., Biochim. Biophys. Acta, 1, 61 (1947). Abul-Fadl, M. A. M., and King, E. J., Biochem. J., 44, 435 (1949) ; Arch. Biochem. and Biophys., 37, 172 (1952).
Sadasivan, V., Nature, 169, 418 (1952).
Thoai, N. v., Roche, J., and Roger, M., Biochim. Biophys. Acta, 1, 61 (1947).
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SADASIVAN, V. Zinc, Ionic Equilibrium and Phosphatase Activity. Nature 170, 421 (1952). https://doi.org/10.1038/170421a0
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DOI: https://doi.org/10.1038/170421a0
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