Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-10-7
pubmed:abstractText
The delta opioid receptor has been purified, in an active form, by succinylmorphine affinity chromatography. The receptor was purified partially from bovine frontal cortex and to apparent homogeneity from neuroblastoma x glioma hybrid NG108-15 cells as observed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by silver staining. Antiserum to the purified bovine receptor inhibited ligand binding to membranes and immunoprecipitated a 58 kDa protein from NG108-15 cells. Reconstitution of the receptor with lipids enhanced binding by 9-fold. The 58 kDa band protein after electroelution and reconstitution with lipids also showed specific binding, indicating that the receptor could be renatured even after SDS-PAGE in an appropriate lipid environment.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
330
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
146-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Purification and reconstitution of the delta opioid receptor.
pubmed:affiliation
Department of Biochemistry, All India Institute of Medical Sciences, New Delhi.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't