{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T23:11:31Z","timestamp":1775085091000,"version":"3.50.1"},"reference-count":19,"publisher":"The Royal Society","issue":"1111","license":[{"start":{"date-parts":[[1976,4,13]],"date-time":"1976-04-13T00:00:00Z","timestamp":198201600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/royalsociety.org\/journals\/ethics-policies\/data-sharing-mining\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1976,4,13]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The fast kinetics of binding of sulphonamides to carbonic anhydrase have been examined. Six homologous series of sulphonamides have been studied. In all cases the increase in binding constant in a homologous series is due mainly to an increase in the association rate constant. Meta- and ortho-substituted sulphonamides have lower binding constants also mainly due to a lower association rate constant. The binding of sulphonamides to apocarbonic anhydrase has been measured by a specific affinity method. The effects of homologous series are largely reproduced on the apoenzyme but the effects of positional isomerization are not; the binding process is pH-insensitive. Evidence is presented that the binding process for sulphonamides and carbonic anhydrase involves an intermediate non-coordinate complex which is then converted into the final coordinate complex. Structure-activity relations in the binding of sulphonamides to carbonic anhydrase are examined on the basis of effects on (a) the stability of the intermediate complex; (b) the rate of isomerization into the coordinate complex; (c) the dissociation rate constant.<\/jats:p>","DOI":"10.1098\/rspb.1976.0034","type":"journal-article","created":{"date-parts":[[2006,12,18]],"date-time":"2006-12-18T18:11:46Z","timestamp":1166465506000},"page":"107-125","source":"Crossref","is-referenced-by-count":67,"title":["Kinetic aspects of structure\u2500activity relations: the binding of sulphonamides by carbonic anhydrase"],"prefix":"10.1098","volume":"193","author":[{"given":"R. W.","family":"King","sequence":"first","affiliation":[{"name":"Division of Molecular Pharmacology, National Institute for Medical Research, London NW7 1AA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Arnold Stanley Vincent","family":"Burgen","sequence":"additional","affiliation":[{"name":"Division of Molecular Pharmacology, National Institute for Medical Research, London NW7 1AA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"175","reference":[{"key":"p_1","first-page":"5137","article-title":"Purification and properties of hum an erythrocyte carbonic anhydrases. biol","volume":"241","author":"Armstrong J .","year":"1966","journal-title":"Chem."},{"key":"p_2","unstructured":"Basolo F. & Pearson It. G. 1967 Mechanisms of inorganic reactions 2nd ed. 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Biochim. biophys","volume":"118","author":"Kernohan J .","year":"1966","journal-title":"Acta"},{"key":"p_10","first-page":"278","article-title":"Sulphonamide complexes of hum an carbonic anhydrases ultraviolet difference spectroscopy. Biochim. biophys","volume":"207","author":"King R. W.","year":"1970","journal-title":"Acta"},{"key":"p_11","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(74)80487-4"},{"key":"p_12","unstructured":"Liljas A. 1971 Crystal structure studies of human erythrocyte carbonic anhydrase C at high resolution. Stockholm: Almqvist & Wiksell."},{"key":"p_13","first-page":"945","article-title":"Effects of pH and inhibitors on some properties related to m etal binding in bovine carbonic anhydrase. J . biol","volume":"238","author":"Lindskog S.","year":"1963","journal-title":"Chem."},{"key":"p_14","doi-asserted-by":"crossref","unstructured":"Lindskog S. & N ym an P. O. 1964 Metal binding properties of hum an erythrocyte carbonic anhydrases. Biochim. biophys. 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