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题名: Identifying and applying a highly selective probe to simultaneously determine the O-glucuronidation activity of human UGT1A3 and UGT1A4
作者: Jiang, Li1;  Liang, Si-Cheng2, 3;  Wang, Chao1;  Ge, Guang-Bo2;  Huo, Xiao-Kui1;  Qi, Xiao-Yi4;  Deng, Sa1;  Liu, Ke-Xin1;  Ma, Xiao-Chi1
刊名: SCIENTIFIC REPORTS
发表日期: 2015-04-17
DOI: 10.1038/srep09627
卷: 5
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Multidisciplinary Sciences
研究领域[WOS]: Science & Technology - Other Topics
英文摘要: Glucuronidation mediated by uridine 59-diphospho (UDP)-glucuronosyltransferase is an important detoxification pathway. However, identifying a selective probe of UDP-glucuronosyltransferase is complicated because of the significant overlapping substrate specificity displayed by the enzyme. In this paper, desacetylcinobufagin (DACB) 3-O- and 16-O-glucuronidation were found to be isoform-specific probe reactions for UGT1A4 and UGT1A3, respectively. DACB was well characterized as a probe for simultaneously determining the catalytic activities of O-glucuronidation mediated by UGT1A3 and UGT1A4 from various enzyme sources, through a sensitive analysis method.
关键词[WOS]: HUMAN UDP-GLUCURONOSYLTRANSFERASES ;  HUMAN LIVER-MICROSOMES ;  DRUG-GLUCURONIDATION ;  N-GLUCURONIDATION ;  MASS-SPECTROMETRY ;  CHROMATOGRAPHY ;  SUBSTRATE ;  ACID ;  IDENTIFICATION ;  AMITRIPTYLINE
语种: 英语
WOS记录号: WOS:000353275700001
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/146159
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Dalian Med Univ, Acad Integrat Med, Coll Pharm, Key Lab Pharmacokinet & Drug Transport Liaoning, Dalian 116044, Peoples R China
2.Chinese Acad Sci, Dalian Inst Chem Phys, Lab Pharmaceut Resource Discovery, Dalian, Peoples R China
3.Chinese Acad Sci, Grad Sch, Beijing, Peoples R China
4.Dalian Med Univ, Affiliated Hosp 2, Dalian 116044, Peoples R China

Recommended Citation:
Jiang, Li,Liang, Si-Cheng,Wang, Chao,et al. Identifying and applying a highly selective probe to simultaneously determine the O-glucuronidation activity of human UGT1A3 and UGT1A4[J]. SCIENTIFIC REPORTS,2015,5.
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