Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1992-9-15
|
pubmed:abstractText |
Self-incompatibility in flowering plants of the family Solanaceae is mediated by the product of the S-allele. The allelic products of the S-gene in the female sexual tissues of the pistil are glycoproteins in the mol. wt range 28-32 kDa. These S-glycoproteins have been isolated from styles of Nicotiana alata, homozygous for the S1- and S2-alleles. Earlier studies have indicated that the single potential N-glycosylation site on the S1-glycoprotein bears a glycan chain, whereas of the four potential N-glycosylation sites on the S2-glycoprotein, three are glycosylated. This paper describes the purification and characterization of the N-linked glycan chains from these two glycoproteins. Oligosaccharides were cleaved off the glycoproteins using peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F (N-glycanase F) and separated by anion-exchange HPLC. Four types of hybrid structure were defined by chemical techniques, fast atom bombardment-mass spectrometry (FAB-MS) and 1H-NMR. Although the relative amounts differed, all four structures were found on both the S1- and S2-glycoproteins, and are heterogeneous at some N-glycosylation sites. No O-linked glycans were detected on the S2-glycoprotein. These results are discussed in relation to the potential of the structural diversity residing in this array of glycoforms to play a rôle in allelic specificity.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0959-6658
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
2
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
241-50
|
pubmed:dateRevised |
2009-9-29
|
pubmed:meshHeading |
pubmed-meshheading:1498421-Alleles,
pubmed-meshheading:1498421-Carbohydrate Sequence,
pubmed-meshheading:1498421-Fertilization,
pubmed-meshheading:1498421-Glycoproteins,
pubmed-meshheading:1498421-Magnetic Resonance Spectroscopy,
pubmed-meshheading:1498421-Molecular Sequence Data,
pubmed-meshheading:1498421-Molecular Structure,
pubmed-meshheading:1498421-Plant Proteins,
pubmed-meshheading:1498421-Plants,
pubmed-meshheading:1498421-Plants, Toxic,
pubmed-meshheading:1498421-Polysaccharides,
pubmed-meshheading:1498421-Spectrometry, Mass, Fast Atom Bombardment,
pubmed-meshheading:1498421-Tobacco
|
pubmed:year |
1992
|
pubmed:articleTitle |
Structural analysis of the N-linked glycan chains from a stylar glycoprotein associated with expression of self-incompatibility in Nicotiana alata.
|
pubmed:affiliation |
Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Victoria, Australia.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|