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dc.contributor.authorHuang, Yi-Longen_US
dc.contributor.authorChung, Tsai-Wenen_US
dc.contributor.authorChang, Chia-Maoen_US
dc.contributor.authorChen, Chih-Hauen_US
dc.contributor.authorLiao, Chen-Chungen_US
dc.contributor.authorTsay, Yeou-Guangen_US
dc.contributor.authorShaw, Gwo-Chyuanen_US
dc.contributor.authorLiaw, Shwu-Hueyen_US
dc.contributor.authorSun, Chung-Mingen_US
dc.contributor.authorLin, Chao-Hsiungen_US
dc.date.accessioned2014-12-08T15:28:10Z-
dc.date.available2014-12-08T15:28:10Z-
dc.date.issued2012-11-01en_US
dc.identifier.issn1618-2642en_US
dc.identifier.urihttp://dx.doi.org/10.1007/s00216-012-6349-0en_US
dc.identifier.urihttp://hdl.handle.net/11536/20399-
dc.description.abstractThe serine hydrolase family consists of more than 200 members and is one of the largest enzyme families in the human genome. Although up to 50 % of this family remains unannotated, there are increasing evidences that activities of certain serine hydrolases are associated with diseases like cancer neoplasia, invasiveness, etc. By now, several activity-based chemical probes have been developed and are applied to profile the global activity of serine hydrolases in diverse proteomes. In this study, two fluorophosphonate (FP)-based chemical probes were synthesized. Further examination of their abilities to label and pull down serine hydrolases was conducted. In addition, the poly-3-hydroxybutyrate depolymerase (PhaZ) from Bacillus thuringiensis was demonstrated as an appropriate standard serine hydrolase, which can be applied to measure the labeling ability and pull-down efficiency of FP-based probes. Furthermore, mass spectrometry (MS) was used to identify the serine residue that covalently bonded to the active probes. Finally, these FP-based probes were shown capable of establishing the serine hydrolase profiles in diverse mouse tissues; the serine hydrolases pulled down from mouse liver organ were further identified by MS. In summary, our study provides an adequate method to evaluate the reactivity of FP-based probes targeting serine hydrolases.en_US
dc.language.isoen_USen_US
dc.subjectActivity-based probeen_US
dc.subjectSerine hydrolaseen_US
dc.subjectPhaZen_US
dc.subjectEsteraseen_US
dc.subjectFluorophosphonateen_US
dc.titleQualitative analysis of the fluorophosphonate-based chemical probes using the serine hydrolases from mouse liver and poly-3-hydroxybutyrate depolymerase (PhaZ) from Bacillus thuringiensisen_US
dc.typeArticleen_US
dc.identifier.doi10.1007/s00216-012-6349-0en_US
dc.identifier.journalANALYTICAL AND BIOANALYTICAL CHEMISTRYen_US
dc.citation.volume404en_US
dc.citation.issue8en_US
dc.citation.spage2387en_US
dc.citation.epage2396en_US
dc.contributor.department應用化學系zh_TW
dc.contributor.departmentDepartment of Applied Chemistryen_US
dc.identifier.wosnumberWOS:000310083900031-
dc.citation.woscount2-
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