beta-Glucosylation of chitooligomers by galactosyltransferase
Language English Country Netherlands Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
9648269
DOI
10.1016/s0008-6215(97)00248-6
PII: S0008-6215(97)00248-6
Knihovny.cz E-resources
- MeSH
- Acetylglucosamine chemistry MeSH
- Antigens, Surface metabolism MeSH
- Killer Cells, Natural chemistry MeSH
- Galactosyltransferases metabolism MeSH
- Glucosides chemical synthesis MeSH
- Binding, Competitive MeSH
- Rats MeSH
- NK Cell Lectin-Like Receptor Subfamily B MeSH
- Lectins, C-Type * MeSH
- Magnetic Resonance Spectroscopy MeSH
- Milk enzymology MeSH
- Molecular Sequence Data MeSH
- Oligosaccharides chemical synthesis MeSH
- Carbohydrate Sequence MeSH
- Cattle MeSH
- Uridine Diphosphate Glucose metabolism MeSH
- Protein Binding physiology MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Acetylglucosamine MeSH
- Antigens, Surface MeSH
- Galactosyltransferases MeSH
- Glucosides MeSH
- NK Cell Lectin-Like Receptor Subfamily B MeSH
- Lectins, C-Type * MeSH
- Oligosaccharides MeSH
- Uridine Diphosphate Glucose MeSH
Galactosyltransferase from bovine milk was found to be able to utilise UDP-Glc to transfer Glc onto GlcNAc and chitooligomers[-beta-GlcNAc-(1-->4)-]n, n = 2-4. beta-Glucosylated products were used in binding studies with NKR-P1A protein cloned from rat natural killer cells.
Carbohydr Res. 2015 Jan 12;401:132 PubMed
References provided by Crossref.org
Nkrp1 family, from lectins to protein interacting molecules
Compounds isolated at the Institute of Microbiology in 1989-2001 and future trends
