Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1990-6-6
pubmed:abstractText
The polyclonal antibody response of the Lewis rat to bovine myelin proteolipid protein (PLP) has been investigated following immunisation with either the purified protein or bovine central nervous system myelin. In both situations, the carboxyl-terminal sequence of PLP was identified as the immunodominant domain of this protein and epitope mapping demonstrated that the carboxyl-terminal amino acid, phenylalanine276, was a critical requirement for antibody recognition of this epitope. This single epitope accounted for approximately 78% and 56% of the antibody response to PLP in rats immunised with PLP or bovine myelin, respectively. Polyclonal rat antibodies specific for this carboxyl terminal epitope of PLP were also obtained following immunisation with a synthetic 20 amino acid oligopeptide analogue of the carboxyl-terminal sequence of PLP. Western blotting demonstrated this antibody response was specific for the PLP and DM-20 components of mammalian central nervous system myelin. In contrast, no major PLP epitopes were detected within the PLP amino acid sequences 35-58 and 91-150, the other major hydrophilic domains of this protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0165-5728
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
155-62
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
The immune response to myelin proteolipid protein in the Lewis rat: identification of the immunodominant B cell epitope.
pubmed:affiliation
Section of Neurology, University of Wales College of Medicine, Heath Park, Cardiff, U.K.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't