Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/60324
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dc.contributor.authorWeng, S.F.en_US
dc.contributor.author翁淑芬zh_TW
dc.contributor.authorChao, Y.F.en_US
dc.contributor.authorLin, J.W.en_US
dc.date2004zh_TW
dc.date.accessioned2014-06-09T05:56:14Z-
dc.date.available2014-06-09T05:56:14Z-
dc.identifier.issn0006-291Xzh_TW
dc.identifier.urihttp://hdl.handle.net/11455/60324-
dc.description.abstractVibrio fischeri ATCC 7744 is an ampicillin resistant (Amp(r)) marine luminous bacterium. The MIC test indicates that V fischeri is highly resistant to penicillins, and susceptible to cephalosporins. V. fischeri ampC gene was cloned and identified. Nucleotide sequence of an unidentified ufo gene and the ampC, ppiB genes (GenBank Accession No. AY438037) has been determined; whereas the ampC gene encodes the beta-lactarnase (AmpC) and the ppiB gene encodes the peptidyl-prolyl cis trans isomerase B. Alignment and comparison show that V. fischeri beta-lactamase is homologous to the related species'. The specific amino acid residues STFK (62nd to 65th), SDN (122nd to 124th), and D (155th) located 34 residues downstream from the SDN loop of the class A beta-lactamases are highly conserved, but the KTG is not found. V fischeri ampC gene encoding beta-lactamase has a calculated M-r 31,181 and comprises 283 amino acid residues (pI 5.35). There is a signal peptide of 18 amino acid residues MKIKPFLFGLIVLANNAI in the pro-beta-lactamase, which functioned for secretion; thus, the matured protein only has M-r 29,197 and comprises 265 amino acid residues (pI 4.95). SDS-PAGE and the beta-lactamase functional assays elicit that the M-r of the beta-lactamases are close to 29 kDa. IEF and the beta-lactamase functional assays show that the beta-lactamases' pi are close to 4.8 as predicted. The results elucidate that V fischeri ampC gene and the cloned ampC gene in Escherichia coli are the same one. The gene order of the ampC and the related genes is -ufo-(P*-intern)-ampC-ppiB--> (P*-intern: intern promoter for sub-regulation), whereas the P*-intern promoter displays the function to lead the ampC gene's expression for stress response. (C) 2003 Elsevier Inc. All rights reserved.en_US
dc.language.isoen_USzh_TW
dc.relationBiochemical and Biophysical Research Communicationsen_US
dc.relation.ispartofseriesBiochemical and Biophysical Research Communications, Volume 314, Issue 3, Page(s) 838-843.en_US
dc.relation.urihttp://dx.doi.org/10.1016/j.bbrc.2003.12.171en_US
dc.subjectampC geneen_US
dc.subjectAmpC (beta-lactamase)en_US
dc.subjectintern promoteren_US
dc.subjectacyl-protein synthetaseen_US
dc.subjectphotobacterium-leiognathien_US
dc.subjectnucleotide-sequenceen_US
dc.subjectlux operonen_US
dc.subjectbacterial bioluminescenceen_US
dc.subjectregulatory regionen_US
dc.subjectxanthomonas-campestrisen_US
dc.subjectescherichia-colien_US
dc.subjectfunctional-analysisen_US
dc.subjectexpressionen_US
dc.titleIdentification and characteristic analysis of the ampC gene encoding beta-lactamase from Vibrio fischerien_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1016/j.bbrc.2003.12.171zh_TW
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