{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,11,20]],"date-time":"2023-11-20T19:38:14Z","timestamp":1700509094269},"reference-count":0,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[1975,5,1]],"date-time":"1975-05-01T00:00:00Z","timestamp":168134400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[1975,5]]},"abstract":"<jats:p>\n            A comparison of the binding of radioactive penicillin G to whole cells and the membrane fraction derived from\n            <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n            KM 338 was made. This organism has intrinsic resistance to penicillin. The binding to the membrane fraction which catalyzed peptidoglycan synthesis followed saturation type kinetics and saturation was achieved at approximately 2 nmol of penicillin G per ml, whereas binding to the whole cells was entirely of the nonsaturation type. The binding of carbenicillin to the membrane fraction was determined by competition between radioactive penicillin G and unlabeled carbenicillin for the binding sites. It was bound at the same sites in almost the same manner. When whole cells were pretreated with high concentration of unlabeled penicillin G or carbenicillin, the subsequent binding of radioactive penicillin G to the membrane fraction from carbenicillin-treated cells was entirely nonspecific, but with penicillin G-pretreated cells it was still specific. There was apparently specific binding of radioactive penicillin G to ethylenediaminetetraacetate-treated cells.\n            <jats:italic>P. aeruginosa<\/jats:italic>\n            KM 338 had an extremely low activity of \u03b2-lactamase compared with other enzyme-producing organisms. This enzyme from\n            <jats:italic>P. aeruginosa<\/jats:italic>\n            KM 338 was of the cephalosporinase type. These data indicate that penicillin resistance of\n            <jats:italic>P. aeruginosa<\/jats:italic>\n            KM 338 may be a consequence of the development of a permeability barrier which prevents the antibiotic from reaching its sites of action in the cytoplasmic membrane.\n          <\/jats:p>","DOI":"10.1128\/aac.7.5.629","type":"journal-article","created":{"date-parts":[[2012,6,27]],"date-time":"2012-06-27T23:57:02Z","timestamp":1340841422000},"page":"629-635","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":18,"title":["Penicillin-Resistant Mechanisms in\n            <i>Pseudomonas aeruginosa<\/i>\n            : Binding of Penicillin to\n            <i>Pseudomonas aeruginosa<\/i>\n            KM 338"],"prefix":"10.1128","volume":"7","author":[{"given":"Hidekazu","family":"Suginaka","sequence":"first","affiliation":[{"name":"Department of Microbiology, Osaka University Dental School, Joan-cho, Kita-ku, Osaka 530, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Akira","family":"Ichikawa","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Osaka University Dental School, Joan-cho, Kita-ku, Osaka 530, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shozo","family":"Kotani","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Osaka University Dental School, Joan-cho, Kita-ku, Osaka 530, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","container-title":["Antimicrobial Agents and Chemotherapy"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.7.5.629","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.7.5.629","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,2,21]],"date-time":"2022-02-21T23:11:36Z","timestamp":1645485096000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/AAC.7.5.629"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1975,5]]},"references-count":0,"journal-issue":{"issue":"5","published-print":{"date-parts":[[1975,5]]}},"alternative-id":["10.1128\/AAC.7.5.629"],"URL":"https:\/\/doi.org\/10.1128\/aac.7.5.629","relation":{},"ISSN":["0066-4804","1098-6596"],"issn-type":[{"value":"0066-4804","type":"print"},{"value":"1098-6596","type":"electronic"}],"subject":[],"published":{"date-parts":[[1975,5]]},"assertion":[{"value":"1975-05-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}