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Semisynthesis of C17:0 isoforms of sulphatide and glucosylceramide using immobilised sphingolipid ceramide N-deacylase for application in analytical mass spectrometry
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SYSNO ASEP 0346664 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Semisynthesis of C17:0 isoforms of sulphatide and glucosylceramide using immobilised sphingolipid ceramide N-deacylase for application in analytical mass spectrometry Author(s) Kuchař, L. (CZ)
Rotková, J. (CZ)
Asfaw, B. (CZ)
Lenfeld, Jiří (UMCH-V) RID
Horák, Daniel (UMCH-V) RID, ORCID
Korecká, L. (CZ)
Bílková, Z. (CZ)
Ledvinová, J. (CZ)Source Title Rapid Communications in Mass Spectrometry. - : Wiley - ISSN 0951-4198
Roč. 24, č. 16 (2010), s. 2393-2399Number of pages 7 s. Language eng - English Country GB - United Kingdom Keywords reverse hydrolysis reaction ; quantitative-determination ; internal standards Subject RIV CB - Analytical Chemistry, Separation R&D Projects GA203/09/0857 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z40500505 - UMCH-V (2005-2011) UT WOS 000280687200011 DOI 10.1002/rcm.4659 Annotation Sphingolipid ceramide N-deacylase (SCDase, EC 3.5.1.69) is a hydrolytic enzyme isolated from Psendomonas sp. TK 4. In addition to its primary deacylation function, this enzyme is able to reacylate lyso-sphingolipids under specific conditions. We immobilized the enzyme on magnetic macroporous cellulose and used it to semisynthesise C17:0 glucosylceramide and C17:0 sulphatide. Workplace Institute of Macromolecular Chemistry Contact Eva Čechová, cechova@imc.cas.cz ; Tel.: 296 809 358 Year of Publishing 2011
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