Abstract
WE have shown previously that carbonic anhydrase is a zinc-protein compound1,2 and this was confirmed by other workers3,4'. That the catalytic activity of carbonic anhydrase, unlike the physiological activity of insulin, depends on the presence of zinc in its molecule is strongly supported by the following considerations. (1) An instantaneous, strong and perfectly reversible inhibition of carbonic anhydrase by very small concentrations of potassium cyanide, hydrogen sulphide and sodium azide which react in this way only with metals. (2) The presence of high concentrations of zinc in purified enzyme preparations obtained by different methods and from different materials. (3) The proportionality between the zinc content of different fractions and their catalytic activity. (4) The absence of other metals from purified enzyme preparations.
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References
Keilin, D., and Mann, T., NATURE, 144, 442 (1939).
Keilin, D., and Mann, T., Biochem. J., 34, 1163 (1940).
Hove, E., Elvehjem, C. A., and Hart, E. B., J. Biol. Chem., 136, 425 (1940).
Scott, D. A., and Mendive, J. R., J. Biol. Chem., 139, 661 (1940) and 140, 445 (1941).
Eirich, F. R., and Rideal, E. K., NATURE, 146, 541 (1940).
Scott, D. A., and Fisher, A. M., J. Biol. Chem., 144, 371 (1942).
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KEILIN, D., MANN, T. Activity of Purified Carbonic Anhydrase. Nature 153, 107–108 (1944). https://doi.org/10.1038/153107a0
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DOI: https://doi.org/10.1038/153107a0
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