Linked Life Data

1426235

Source:http://linkedlifedata.com/resource/pubmed/id/1426235

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-12-2
pubmed:abstractText
A high pH anion exchange chromatographic (HPAEC) system for the separation of isomeric sialo-oligosaccharide products was developed. Employing this system, using Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6Man beta 1-->4GlcNAc as a substrate, a Gal beta 1-->4GlcNAc-R alpha 2-->3-sialyltransferase activity was detected for the first time in human liver. This activity is expressed together with the prevalent alpha 2-->6-sialyltransferase. Furthermore, in addition to the major alpha 2-->3-sialyltransferase, a low but distinct activity of alpha 2-->6-sialyltransferase was detected in human placenta. This activity could not be found by methods based on methylation analysis or high resolution NMR spectroscopy. It is concluded that HPAEC, in combination with the use of the pentasaccharide as an acceptor substrate, is suited for the specific detection of minor, Gal beta 1-->4GlcNAc-specific sialyltransferase activities.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
312
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Human liver and human placenta both contain CMP-NeuAc:Gal beta 1-->4GlcNAc-R alpha 2-->3- as well as alpha 2-->6-sialyltransferase activity.
pubmed:affiliation
Department of Medical Chemistry, Vrije Universiteit, Amsterdam, The Netherlands.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't