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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16-17
|
pubmed:dateCreated |
1983-3-24
|
pubmed:abstractText |
The properties of a mouse monoclonal antibody to beta-endorphin secreted by a clone of hybrid myelomas (3-E7) are described. The antibody displays virtually complete cross-reactivity to met-enkephalin and leu-enkephalin, but no cross-reactivity to beta-lipotropin, alpha-N-acetyl-beta-endorphin and des-Tyr1-beta-endorphin. Substantial cross-reactivity is seen with some other naturally occurring opioid peptides bearing the enkephalin sequence, such as dynorphin, alpha-neo-endorphin and BAM 22, but cross-reactivity is lacking in the case of certain synthetic enkephalin derivatives possessing a D-amino acid in position 2. The data indicate that for the binding of an antigen to the antibody the N-terminal tyrosine moiety is essential. The antibody recognizes, thus, a site which is of functional significance for the interaction of many naturally occurring opioid peptides with the opiate receptor.
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pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:issn |
0024-3205
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
31
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1721-4
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading | |
pubmed:articleTitle |
Characteristics of a monoclonal beta-endorphin antibody recognizing the N-terminus of opioid peptides.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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