Part of the Biological Council book series (BCSDA)
Structure and function of carbonic anhydrase: comparative studies of sulphonamide binding to human erythrocyte carbonic anhydrases B and C
Soon after the discovery of carbonic anhydrase from bovine erythrocytes (E.C.220.127.116.11), 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.
KeywordsCarbonic Anhydrases Complete Amino Acid Sequence Active Site Region ORTEP Drawing Swedish Natural Science Research Council
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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