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Article: Probing of bismuth antiulcer drug targets in H. pylori by laser ablation - inductively coupled plasma mass spectrometry

TitleProbing of bismuth antiulcer drug targets in H. pylori by laser ablation - inductively coupled plasma mass spectrometry
Authors
Issue Date2012
PublisherRoyal Society of Chemistry. The Journal's web site is located at http://www.rsc.org/Publishing/Journals/MT/About.asp
Citation
Metallomics, 2012, v. 4, p. 277-283 How to Cite?
AbstractA method that allows partial denaturation of protein ligands in Bi- and Zn-protein complexes, leaving the metal coordination centre intact, was developed. It was based on the reduction of the S-S bridges with tris(2-carboxyl)phosphine followed by derivatization with iodoacetamide. Consequently conditions that allow the separation of Bi- and Zn-protein complexes using SDS electrophoresis were found. The separation efficiency was much higher than that in non-denaturating blue native electrophoresis. The method allowed the detection of seven Bi-binding protein candidates in H. pylori treated with bismuth subcitrate, some of which - fructose-bisphosphate aldolase (33.6 kDa), urease alpha subunit (26.4 kDa), and the 16.8 kDa proteins: 30S ribosomal protein S6 and neutrophil activating protein (NapA) - were bio-induced during the treatment. The method also allowed the monitoring of the changes in the Zn-proteome during treatment of H. pylori with the Bi-drug, which was found to increase the concentration of the Zn-binding proteins with particularly strong expression of the urease, S-adenosylmethionine synthetase and the above 16.8 kDa proteins. © 2012 The Royal Society of Chemistry.
Persistent Identifierhttp://hdl.handle.net/10722/159377
ISSN
2015 Impact Factor: 3.54
2015 SCImago Journal Rankings: 1.120
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorTsang, CNen_US
dc.contributor.authorBianga, Jen_US
dc.contributor.authorSun, Hen_US
dc.contributor.authorSzpunar, Jen_US
dc.contributor.authorLobinski, Ren_US
dc.date.accessioned2012-08-16T05:48:56Z-
dc.date.available2012-08-16T05:48:56Z-
dc.date.issued2012en_US
dc.identifier.citationMetallomics, 2012, v. 4, p. 277-283en_US
dc.identifier.issn1756-5901en_US
dc.identifier.urihttp://hdl.handle.net/10722/159377-
dc.description.abstractA method that allows partial denaturation of protein ligands in Bi- and Zn-protein complexes, leaving the metal coordination centre intact, was developed. It was based on the reduction of the S-S bridges with tris(2-carboxyl)phosphine followed by derivatization with iodoacetamide. Consequently conditions that allow the separation of Bi- and Zn-protein complexes using SDS electrophoresis were found. The separation efficiency was much higher than that in non-denaturating blue native electrophoresis. The method allowed the detection of seven Bi-binding protein candidates in H. pylori treated with bismuth subcitrate, some of which - fructose-bisphosphate aldolase (33.6 kDa), urease alpha subunit (26.4 kDa), and the 16.8 kDa proteins: 30S ribosomal protein S6 and neutrophil activating protein (NapA) - were bio-induced during the treatment. The method also allowed the monitoring of the changes in the Zn-proteome during treatment of H. pylori with the Bi-drug, which was found to increase the concentration of the Zn-binding proteins with particularly strong expression of the urease, S-adenosylmethionine synthetase and the above 16.8 kDa proteins. © 2012 The Royal Society of Chemistry.-
dc.languageengen_US
dc.publisherRoyal Society of Chemistry. The Journal's web site is located at http://www.rsc.org/Publishing/Journals/MT/About.aspen_US
dc.relation.ispartofMetallomicsen_US
dc.titleProbing of bismuth antiulcer drug targets in H. pylori by laser ablation - inductively coupled plasma mass spectrometryen_US
dc.typeArticleen_US
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1756-5901&volume=4&spage=277&epage=283&date=2012&atitle=Probing+of+bismuth+antiulcer+drug+targets+in+<i>H.+pylori</i>+by+laser+ablation+–+inductively+coupled+plasma+mass+spectrometryen_US
dc.identifier.emailSun, H: hsun@hku.hken_US
dc.identifier.authoritySun, H=rp00777en_US
dc.identifier.doi10.1039/c2mt00169a-
dc.identifier.pmid22286050-
dc.identifier.scopuseid_2-s2.0-84863392979-
dc.identifier.hkuros205078en_US
dc.identifier.volume4en_US
dc.identifier.spage277en_US
dc.identifier.epage283en_US
dc.identifier.isiWOS:000300886700006-

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