Linked Life Data

1690268

Source:http://linkedlifedata.com/resource/pubmed/id/1690268

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1990-4-20
pubmed:abstractText
Immunochemical analysis of the myelin proteolipid protein (PLP) has identified the carboxyl terminal amino acid phenylalanine 276 as the only PLP epitope conserved between the PLP components of rat and lungfish, species representing the phylogenetically most widely separated groups that synthesise typical CNS myelin. Immunoblotting using a rabbit antiserum raised against the carboxyl terminal sequence of rat PLP (residues 257-276) identified this epitope on the PLP components of both tetrapod (rat, chicken, lizard, and frog) and lobe-finned fish (coelacanth and lungfish) CNS myelin, including the DM-20 isoform of PLP, which is restricted to rat, chicken, and lizard CNS myelin. The conservation of the carboxyl terminus of PLP during evolution suggests this structure may play an important role in maintaining the organisation and function of PLP in the myelin membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1354-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Conservation of the carboxyl terminal epitope of myelin proteolipid protein in the tetrapods and lobe-finned fish.
pubmed:affiliation
Section of Neurology, University of Wales College of Medicine, Cardiff.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't