Linked Life Data

3968060

Source:http://linkedlifedata.com/resource/pubmed/id/3968060

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-3-6
pubmed:abstractText
Polysialosyl chains containing alpha 2-8-linked N-acetylneuraminic acid have been suggested to modulate the biological activity of a neural cell adhesion molecule. Polysialosyl glycopeptides isolated from developing brain were incubated with a bacteriophage containing endosialidase. Sialic acid oligomers up to 7 residues long were liberated both from the glycopeptides and colominic acid. The substrate specificity of the endosialidase was studied with sialic acid oligomers of different sizes prepared from colominic acid. It was found that the endosialidase required the simultaneous presence adjacent to the site of cleavage a minimum of 3 sialic acid residues on the distal side and a minimum of 5 sialic acid residues on the proximal (reducing end) side. From the fragments liberated by the enzyme the existence of polysialic acid chains up to at least 12 residues long in the glycopeptides were concluded. This was also supported by the interaction of the glycopeptides with a meningococcal group B polysaccharide antiserum, which was found to require 10 residues or more for binding. The results indicate that the brain polysialosyl glycopeptides contain a long polysialic acid segment, which is also specifically needed for certain molecular interactions. The implications of the findings for the biological properties of the neural cell adhesion molecule are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
260
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1265-70
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Cleavage of the polysialosyl units of brain glycoproteins by a bacteriophage endosialidase. Involvement of a long oligosaccharide segment in molecular interactions of polysialic acid.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't