Linked Life Data

6083474

Source:http://linkedlifedata.com/resource/pubmed/id/6083474

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1985-2-4
pubmed:abstractText
The interaction of human myelin basic protein with lipophilin has been demonstrated by affinity chromatography. The interaction was specific since neither basic protein, nor albumin bound to an affinity column consisting of BP bound to agarose. Conversely an albumin affinity column failed to bind BP. The pH dependency of the interaction correlated with the known pK for histidine. By the use of large peptides formed by tryptophanyl cleavage by BNPS-skatole, peptide 1-117 bound to the BP affinity column while neither the smaller peptide, 118-170, nor the synthetic nonapeptide bound. The large fragment contains 9 of the 10 histidines in the molecule which may explain the binding of this fragment. The result of such protein-protein interactions makes available a large number of new antigenic sites and extends considerably the range of encephalitogens for disease induction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0364-3190
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1523-31
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Interaction between human myelin basic protein and lipophilin.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't