Linked Life Data

8257853

Source:http://linkedlifedata.com/resource/pubmed/id/8257853

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-1-19
pubmed:abstractText
In a previous study, we determined the structures of the glycans present in ancrod, a thrombin-like serine protease from the venom of the Malayan pit viper Agkistrodon rhodostoma (Pfeiffer et al. (1992) Eur J Biochem 205:961-78). In order to allocate the various carbohydrate chains to distinct N-glycosylation sites of the molecule, we have now isolated individual glycopeptides. Peptide moieties were identified after deglycosylation with peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F by amino acid analysis and sequencing. Liberated oligosaccharides were assigned to the previously deduced carbohydrate structures by high performance liquid chromatography. Although only quantitative differences were observed, the results indicate that each glycosylation site of ancrod carries its characteristic oligosaccharide pattern. Furthermore, all potential sites were shown to be substituted by carbohydrates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0282-0080
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
240-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Glycosylation of the thrombin-like serine protease ancrod from Agkistrodon rhodostoma venom. Oligosaccharide substitution pattern at each N-glycosylation site.
pubmed:affiliation
Biochemisches Institut am Klinikum der Universität, Giessen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't