|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
8
|
|
pubmed:dateCreated |
1990-5-24
|
|
pubmed:abstractText |
We synthesized several chimeric peptides in which the N-terminal nine residues of dynorphin-32, a peptide selective for the kappa opioid receptor, were replaced by opioid peptides selective for other opioid receptor types. Each chimeric peptide retained the high affinity and type selectivity characteristic of its N-terminal sequence. The common C-terminal two-thirds of the chimeric peptides served as an epitope recognized by the same monoclonal antibody. When bound to receptors on a cell surface or membrane preparation, these peptides could still bind specifically to the monoclonal antibody. These chimeric peptides should be useful for isolating mu, delta, and kappa opioid receptors and for identifying opioid receptors on transfected cells in expression cloning procedures. The general approach using chimeric peptides should be applicable to other peptide receptors.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2158105-218947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2158105-2437578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2158105-2544892,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2158105-2549383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2158105-2860615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2158105-2902630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2158105-6118865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2158105-6118870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2158105-6127674,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2158105-6291693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2158105-6310598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2158105-7287299
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
0027-8424
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
87
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
3180-4
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:2158105-Amino Acid Sequence,
pubmed-meshheading:2158105-Animals,
pubmed-meshheading:2158105-Antibodies, Monoclonal,
pubmed-meshheading:2158105-Binding, Competitive,
pubmed-meshheading:2158105-Brain,
pubmed-meshheading:2158105-Cell Membrane,
pubmed-meshheading:2158105-Chimera,
pubmed-meshheading:2158105-Endorphins,
pubmed-meshheading:2158105-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:2158105-Guinea Pigs,
pubmed-meshheading:2158105-Kinetics,
pubmed-meshheading:2158105-Molecular Sequence Data,
pubmed-meshheading:2158105-Receptors, Opioid,
pubmed-meshheading:2158105-Structure-Activity Relationship
|
|
pubmed:year |
1990
|
|
pubmed:articleTitle |
Chimeric opioid peptides: tools for identifying opioid receptor types.
|
|
pubmed:affiliation |
Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
