Condensation reactions catalyzed by ?-N-acetylgalactosaminidase from Aspergillus niger yielding a-N-acetylgalactosaminides
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F10%3A00340836" target="_blank" >RIV/61388971:_____/10:00340836 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Condensation reactions catalyzed by ?-N-acetylgalactosaminidase from Aspergillus niger yielding a-N-acetylgalactosaminides
Original language description
Extracellular a-N-acetylgalactosaminidase from Aspergillus niger catalyzed glycosylation yielding a series of 2-acetamido-2-deoxy-a-D-galactobiosides using 2-acetamido-2-deoxy-D-galactopyranose as a glycosyl donor. The isomers a-D-GalpNAc-D-GalpNAc, a-D-GalpNAc-D-GalpNAc and a-D-GalpNAc-D-GalfNAc were isolated and spectrally characterized. The purified enzyme was further used for the glycosylation of free amino acids (serine and threonine) and their N-(tert-butoxycarbonyl)-protected analogs to synthesize the Tn antigen (GalpNAc-a-O-Ser/Thr) and its N-(tertbutoxycarbonyl)-protected derivatives
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
EE - Microbiology, virology
OECD FORD branch
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Result continuities
Project
<a href="/en/project/OC%20136" target="_blank" >OC 136: Combined chemical and enzymatic synthesis of complex multivalent glycoconjungates - ways to new materials and glycodrugs</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2010
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biocatalysis and Biotransformation
ISSN
1024-2422
e-ISSN
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Volume of the periodical
28
Issue of the periodical within the volume
2
Country of publishing house
GB - UNITED KINGDOM
Number of pages
6
Pages from-to
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UT code for WoS article
000274855300008
EID of the result in the Scopus database
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