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Structure and function of carbonic anhydrase: comparative studies of sulphonamide binding to human erythrocyte carbonic anhydrases B and C

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Drug Action at the Molecular Level

Part of the book series: Biological Council ((BCSDA))

Abstract

Soon after the discovery of carbonic anhydrase from bovine erythrocytes (E.C.4.2.1.1), which catalyses the reaction

by Meldrum and Roughton (1932) it was shown by Mann and Keilin (1940) that certain sulphonamides were specific and potent inhibitors of this enzyme. It has been well documented (see Maren, 1967, for an extensive review on inhibition and physiology, and Lindskog et al. 1971, and Coleman, 1971, for general reviews on carbonic anhydrases) that aromatic and heterocyclic sulphonamides with unsubstituted R—SO2 NH2 groups constitute a class of powerful inhibitors, while aliphatic sulphonamides are poor inhibitors of the carbonic anhydrases.

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Author information

Authors and Affiliations

  1. Department of Molecular Biology, Wallenberg Laboratory, Uppsala University, Uppsala, Sweden

    K. K. Kannan, I. Vaara, B. Notstrand, S. Lövgren, A. Boren, K. Fridborg & M. Petef

Authors
  1. K. K. Kannan
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  2. I. Vaara
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  3. B. Notstrand
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  4. S. Lövgren
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  5. A. Boren
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  6. K. Fridborg
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  7. M. Petef
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Editor information

Editors and Affiliations

  1. National Institute for Medical Research, Mill Hill, London

    G. C. K. Roberts

Copyright information

© 1977 Institute of Biology Endowment Trust Fund

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Kannan, K.K. et al. (1977). Structure and function of carbonic anhydrase: comparative studies of sulphonamide binding to human erythrocyte carbonic anhydrases B and C. In: Roberts, G.C.K. (eds) Drug Action at the Molecular Level. Biological Council. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-03230-3_4

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