Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F12%3A00377487" target="_blank" >RIV/61388971:_____/12:00377487 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.3762/bjoc.8.80" target="_blank" >http://dx.doi.org/10.3762/bjoc.8.80</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3762/bjoc.8.80" target="_blank" >10.3762/bjoc.8.80</a>
Alternative languages
Result language
angličtina
Original language name
Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment
Original language description
The importance of glycans in biological systems is highlighted by their various functions in physiological and pathological processes. Many glycan epitopes on glycoproteins and glycolipids are based on N-acetyllactosamine units (LacNAc; Gal beta 1,4GlcNAc) and often present on extended poly-LacNAc glycans ([Gal beta 1,4GlcNAc](n)). Poly-LacNAc itself has been identified as a binding motif of galectins, an important class of lectins with functions in immune response and tumorigenesis. Therefore, the synthesis of natural and modified poly-LacNAc glycans is of specific interest for binding studies with galectins as well as for studies of their possible therapeutic applications. We present the oxidation by galactose oxidase and subsequent chemical or enzymatic modification of terminal galactose and N-acetylgalactosamine residues of poly-N-acetyllactosamine (poly-LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) by galactose oxidase
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/OC09045" target="_blank" >OC09045: Selective enzymatic oxidations and deracemizations of natural products and biomolecules</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Beilstein Journal of Organic Chemistry
ISSN
1860-5397
e-ISSN
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Volume of the periodical
8
Issue of the periodical within the volume
MAY 9 2012
Country of publishing house
DE - GERMANY
Number of pages
14
Pages from-to
712-725
UT code for WoS article
000303799000001
EID of the result in the Scopus database
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