{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T22:16:57Z","timestamp":1770761817049,"version":"3.50.0"},"reference-count":0,"publisher":"SAGE Publications","issue":"1","license":[{"start":{"date-parts":[[2002,3,1]],"date-time":"2002-03-01T00:00:00Z","timestamp":1014940800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Microbial Drug Resistance"],"published-print":{"date-parts":[[2002,3]]},"abstract":"<jats:p>\n                    <jats:italic toggle=\"yes\">Pseudomonas aeruginosa<\/jats:italic>\n                    802 was isolated at Rabta hospital in Tunis and was resistant to extended-spectrum cephalosporins and aztreonam. It produced a pI 7.6 extended-spectrum\n                    <jats:italic toggle=\"yes\">\u03b2<\/jats:italic>\n                    -lactamase\n         (ESBL). The ESBL, named LBT 802, was purified to homogeneity by filtration on Sephadex G-75 followed by CM-Sepharose chromatography and high-performance liquid chromatography (HPLC) on a TSK-gel SP-5PW\n         column. The LBT 802 enzyme had a molecular mass of 30 kDa. It showed a broad-substrate profile by hydrolyzing benzylpenicillin, ampicillin, cephalothin, cephaloridine, cefotaxime, ceftriaxone, and cefpirome\n         but not ceftazidime, cefoxitin, imipenem, or aztreonam. The highest hydrolytic efficiency (\n                    <jats:italic toggle=\"yes\">V<\/jats:italic>\n                    <jats:sub>max<\/jats:sub>\n                    \/\n                    <jats:italic toggle=\"yes\">K<\/jats:italic>\n                    <jats:sub>m<\/jats:sub>\n                    ) was obtained for ampicillin, cephalothin, cephaloridine, and benzylpenicillin.\n         Among extended-spectrum cephalosporins the best substrate was ceftriaxone followed by cefotaxime and cefpirome. LBT 802 activity was inhibited by clavulanic acid, sulbactam, imipenem, cefoxitin, and aztreonam.\n         It showed its lowest\n                    <jats:italic toggle=\"yes\">K<\/jats:italic>\n                    <jats:sub>i<\/jats:sub>\n                    values for clavulanic acid, imipenem and sulbactam.\n                  <\/jats:p>","DOI":"10.1089\/10766290252913700","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T18:11:48Z","timestamp":1027707108000},"page":"9-13","source":"Crossref","is-referenced-by-count":8,"title":["Biochemical Characterization of a Novel Extended-Spectrum\n                    <i>\u03b2<\/i>\n                    -Lactamase from\n                    <i>Pseudomonas aeruginosa<\/i>\n                    802"],"prefix":"10.1177","volume":"8","author":[{"given":"Samia","family":"Rejiba","sequence":"first","affiliation":[{"name":"Laboratoire de Biochimie et de Technobiologie, Facult\u00e9 des Sciences de Tunis, Tunis, Tunisia."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ferid","family":"Limam","sequence":"additional","affiliation":[{"name":"Laboratoire de Biochimie et de Technobiologie, Facult\u00e9 des Sciences de Tunis, Tunis, Tunisia."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cherifa","family":"Belhadj","sequence":"additional","affiliation":[{"name":"Laboratoire de Biochimie et de Technobiologie, Facult\u00e9 des Sciences de Tunis, Tunis, Tunisia."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Omrane","family":"Belhadj","sequence":"additional","affiliation":[{"name":"Laboratoire de Biochimie et de Technobiologie, Facult\u00e9 des Sciences de Tunis, Tunis, Tunisia."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kamel","family":"Ben-Mahrez","sequence":"additional","affiliation":[{"name":"Laboratoire de Biochimie et de Technobiologie, Facult\u00e9 des Sciences de Tunis, Tunis, Tunisia."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"179","published-online":{"date-parts":[[2002,3]]},"container-title":["Microbial Drug Resistance"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.sagepub.com\/doi\/pdf\/10.1089\/10766290252913700","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.sagepub.com\/doi\/pdf\/10.1089\/10766290252913700","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T18:13:59Z","timestamp":1770747239000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.sagepub.com\/doi\/full\/10.1089\/10766290252913700"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,3]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2002,3]]}},"alternative-id":["10.1089\/10766290252913700"],"URL":"https:\/\/doi.org\/10.1089\/10766290252913700","relation":{},"ISSN":["1076-6294","1931-8448"],"issn-type":[{"value":"1076-6294","type":"print"},{"value":"1931-8448","type":"electronic"}],"subject":[],"published":{"date-parts":[[2002,3]]}}}