Linked Life Data

6197305

Source:http://linkedlifedata.com/resource/pubmed/id/6197305

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1984-2-24
pubmed:abstractText
By affinity chromatography on concanavalin A (ConA) linked to Sepharose, S-carboxymethylated rat alpha-fetoprotein could be separated into two molecular variants: a ConA-reactive and a ConA-nonreactive fraction. The carbohydrate chains were quantitatively released from the protein by hydrazinolysis. Based on methylation analysis and high-resolution 1H-NMR spectroscopy of the re-N-acetylated hydrazinolysates, the carbohydrate structures of the two ConA-molecular variants of alpha-fetoprotein were established. The ConA-reactive species contains two N-glycosidic carbohydrate units per molecule, both having the following structure: (formula; see text) The ConA-nonreactive species possesses also two N-glycosidically linked oligosaccharide chains per molecule; each of these has the following structure: (formula; see text)
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
137
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
319-23
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Structure determination of the carbohydrate chains of rat alpha-fetoprotein.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't