Linked Life Data

11062987

Source:http://linkedlifedata.com/resource/pubmed/id/11062987

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2000-11-30
pubmed:abstractText
The 32 kDa enamelin protein isolated from developing porcine enamel was previously shown to contain eight different asparagine-linked oligosaccharides. However, only three consensus attachment sites were evident in this protein. In this study, glycopeptides containing all three potential glycosylation sites (72-Asn, 79-Asn and 91-Asn) were purified from 32 kDa enamelin. The oligosaccharides were isolated from each glycopeptide following digestion with N-oligosaccharide glycopeptidase, labeled with 2-aminopyridine at the reducing ends, and then characterized by reverse phase HPLC. All three potential sites were found to be glycosylated heterogeneously (i.e., five biantennary complexes at 72-Asn, two biantennary complexes at 79-Asn, three triantennary complexes at 91-Asn), accounting for all eight oligosaccharides characterized previously. These results indicate that 32 kDa enamelin has a complex pattern of asparagine-linked glycosylation localized within a small region (20 residues) of the protein. The functional significance of this glycosylation remains to be established.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-8207
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
39-46; discussion 63-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Sites of asparagine-linked oligosaccharides in porcine 32 kDa enamelin.
pubmed:affiliation
Department of Biochemistry, School of Dental Medicine, Tsurumi University, Yokohama, Japan.
pubmed:publicationType
Journal Article