Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-5-4
pubmed:abstractText
It has been reported that the acetylcholine receptor may be used by the rabies virus to concentrate at sites in proximal to peripheral nerves. It has also been reported that the binding site for the receptor is located within the 190-203 region of the virus glycoprotein on the basis of its structural homology with the toxic center of snake neurotoxins, which are well known cholinergic ligands. We prepared monoclonal antibodies against the synthetic tetradecapeptide having the same sequence as the putative binding site of the rabies virus. One of three antibodies (clone 2PV 36-74) was able to recognize both the whole virus and its peplomeric glycoprotein and could bind acetylcholine. It was also able to inhibit the binding both of alpha-bungarotoxin and rabies virus glycoprotein to the acetylcholine receptor. We have covalently bound 2PV 36-74 to an HPLC affinity column and utilized it for specific purification of rabies virus glycoprotein. The immunoaffinity chromatographic method we describe is very sensitive and highly specific. Moreover this procedure does not denature the sample and is vary rapid and efficient.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-1759
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
127
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
131-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
HPLC immunoaffinity purification of rabies virus glycoprotein using immobilized antipeptide antibodies.
pubmed:affiliation
CRISMA, Centro Didattico dell'Università, Siena, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't