Abstract
IT was shown by Henriques1 that the rate at which carbon dioxide is evolved in the reaction H2CO3⇌ CO2 + H2O is greatly accelerated by the presence of laked blood, mere traces of which are sufficient to catalyse this reaction4. That this acceleration is not due to hæmoglobin was clearly demonstrated by Meldrum and Roughton3,4 who have separated from the red blood corpuscles a now enzyme capable of catalysing both phases of the above reaction. They described this enzyme under the name of carbonic anhydrase and gave a detailed account of its properties. Their purified preparation of this enzyme was a colourless substance, very active and sensitive to KCN, H2S and NaN3. The amount of this enzyme-preparation was, however, very small and scarcely sufficient even to recognize it with certainty as a protein compound. In the course of our study of metallo-protein compounds5 present in the red blood corpuscles, we have found that the fractions of our preparations left after the complete removal of hæmocuprein had a very high content of zinc and a high carbonic anhydrase activity. By adapting our methods of purification to preparations on larger scale, such as 10 litres of blood at a time, and taking special care to increase the yield of the zinc fraction, we have obtained a highly active preparation of carbonic anhydrase. The activities of different fractions have been tested both by the manometric ‘boat’ method3 and the colorimetric method6. The zinc in different fractions was determined by the dithizone and by the iodometric ferricyanide methods and was also isolated as a crystalline zinc quinaldinat salt.
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References
Henriques, O., Biochem. Z., 200, 1 (1928).
Brinkman, R., and Margaria, E., J. Physiol., 72, 6P (1931).
Meldrum, N. U., and Roughton, F., J. Physiol., 80, 113 and 143 (1931).
Mann, T., and Keilin, D., Proc. Roy Soc., B, 126, 303 (1938).
Philpot, F., and Philpot, J., Biochem. J., 30, 2191 (1936).
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KEILIN, D., MANN, T. Carbonic Anhydrase. Nature 144, 442–443 (1939). https://doi.org/10.1038/144442b0
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DOI: https://doi.org/10.1038/144442b0
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