{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,5,10]],"date-time":"2023-05-10T17:18:26Z","timestamp":1683739106555},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1975,4,1]]},"abstract":"<jats:p>The addition of Zn2+ to human carbonic anhydrase B holoenzyme was shown to enhance the protein fluorescence, and this enhancement was correlated with the inhibition of the p-nitrophenyl acetate esterase activity. The affinity for the inhibitory Zn2+ was increased when the ionic inhibitors, acetate or chloride, were added, suggesting that the inhibitory Zn2+-binding site is within the region of the protein that undergoes an anion-induced conformational change. A similar fluorescence enhancement was observed when Zn2+ was added to human carbonic anhydrase C and to bovine carbonic anhydrase, demonstrating that the binding site is not a thiol group. Circular-dichroism studies showed that the C isoenzyme but not the B isoenzyme underwent a major conformational change in the presence of Zn2+. A mechanism for the Zn2+-induced fluorescence enhancement was suggested on the basis of studies with simple compounds.<\/jats:p>","DOI":"10.1042\/bj1470037","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T19:57:34Z","timestamp":1439236654000},"page":"37-43","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["The effect of zinc on the activity and fluorescence of carbonic anhydrase holoenzymes"],"prefix":"10.1042","volume":"147","author":[{"given":"T R","family":"Hesketh","sequence":"first","affiliation":[{"name":"National Institute for Medical Research, Mill Hill, London NW7 1AA, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M T","family":"Flanagan","sequence":"additional","affiliation":[{"name":"National Institute for Medical Research, Mill Hill, London NW7 1AA, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/147\/1\/37\/563741\/bj1470037.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/147\/1\/37\/563741\/bj1470037.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T16:20:08Z","timestamp":1637943608000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/147\/1\/37\/9479\/The-effect-of-zinc-on-the-activity-and"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1975,4,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1975,4,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1470037","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1975,4,1]]}}}