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dc.contributor.authorChien, Wei-Tingen_US
dc.contributor.authorLiang, Chien-Fuen_US
dc.contributor.authorYu, Ching-Chingen_US
dc.contributor.authorLin, Chien-Hungen_US
dc.contributor.authorLi, Si-Pengen_US
dc.contributor.authorPrimadona, Indahen_US
dc.contributor.authorChen, Yu-Juen_US
dc.contributor.authorMong, Kwok Kong T.en_US
dc.contributor.authorLin, Chun-Chengen_US
dc.date.accessioned2014-12-08T15:35:56Z-
dc.date.available2014-12-08T15:35:56Z-
dc.date.issued2014en_US
dc.identifier.issn1359-7345en_US
dc.identifier.urihttp://hdl.handle.net/11536/24312-
dc.identifier.urihttp://dx.doi.org/10.1039/c4cc01227een_US
dc.description.abstractA simple and efficient protocol for the preparative-scale synthesis of various lengths of oligo-N-acetyllactosamine (oligo-LacNAc) and its multi-sialylated extensions is described. The strategy utilizes one thermophilic bacterial thymidylyltransferase (RmlA) coupled with corresponding sugar-1-phosphate kinases to generate two uridine diphosphate sugars, UDP-galactose and UDP-N-acetylglucosamine. By incorporating glycosyltransferases, oligo-LacNAcs and their sialylated analogs were synthesized.en_US
dc.language.isoen_USen_US
dc.titleSequential one-pot enzymatic synthesis of oligo-N-acetyllactosamine and its multi-sialylated extensionsen_US
dc.typeArticleen_US
dc.identifier.doi10.1039/c4cc01227een_US
dc.identifier.journalCHEMICAL COMMUNICATIONSen_US
dc.citation.volume50en_US
dc.citation.issue43en_US
dc.citation.spage5786en_US
dc.citation.epage5789en_US
dc.contributor.department應用化學系zh_TW
dc.contributor.departmentDepartment of Applied Chemistryen_US
dc.identifier.wosnumberWOS:000335554300028-
dc.citation.woscount1-
Appears in Collections:Articles


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