Linked Life Data

78502

Source:http://linkedlifedata.com/resource/pubmed/id/78502

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1978-8-28
pubmed:abstractText
From experiments with glycoproteins containing the glycopeptide linkages, arabinose-O-hydroxyproline and galactose-O-serine (plant cell wall glycopeptides), N-acetylgalactosamine-O-serine/threonine (pig submaxillary mucin), and N-acetyl-glucosamine-N-asparagine (fetuin), it is apparent that anhydrous liquid HF, a reagent commonly used by snythetic peptide chemists for the complete removal of protecting groups from synthetic peptides, cleaves the O-glycosidic linkages of neutral sugars in 1 hr at 0 degrees C, and the O-glycosidic linkages of amino sugars in 3 hr at 23 degrees C. The N-glycosidic linkage of N-acetylglucosamine to asparagine is not cleaved under any conditions that have been tested. Sodium dodecyl sulfate gel electrophoresis of bovine serum albumin treated in HF does not show any degradation of peptide bonds. Some relatively stable enzymes (lysozyme and RNase) have been shown by others to retain most of their enzymic activity after short treatment (1 hr at 0 degrees C) in HF. With the specificity of HF at 0 degrees C for neutral sugars it should be possible to generate di- or trisaccharides in high yield from polysaccharides containing both neutral and amino sugars with neutral sugars as the reducing termini.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0361-7742
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
553-61
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
A new approach to the structural determination of glycoproteins and polysaccharides: anhydrous HF solvolysis.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.