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AbstractAbstract
[en] A mu-specific opioid receptor was purified to apparent homogeneity from rat brain membranes by 6-succinylmorphine affinity chromatography, Ultrogel filtration, wheat germ agglutinin affinity chromatography, and isoelectric focusing. The purified receptor had a molecular weight of 58,000 as determined by polyacrylamide gel electrophoresis, and was judged to be homogeneous by the following criteria: (1) a single band on the SDS gel; and (2) a specific opioid binding activity of 17,720 pmole/mg protein, close to the theoretical value. In addition, the 58,000 molecular weight value agrees closely with that determined by covalently labelling purified receptor with bromoacetyl-3H-dihydromorphine or with 125I-beta-endorphin and dimethyl suberimidate. To their knowledge, this is the first complete purification of an opioid receptor that retains its ability to bind opiates
Primary Subject
Source
70. annual meeting of the Federation of American Society for Experimental Biology; St. Louis, MO (USA); 13-18 Apr 1986; CONF-8604222--
Record Type
Journal Article
Literature Type
Conference
Journal
Federation Proceedings. Federation of American Societies for Experimental Biology; ISSN 0014-9446;
; CODEN FEPRA; v. 45(4); p. 800

Country of publication
ANIMALS, BETA DECAY RADIOISOTOPES, BODY, CELL CONSTITUENTS, CENTRAL NERVOUS SYSTEM, CENTRAL NERVOUS SYSTEM AGENTS, DAYS LIVING RADIOISOTOPES, DRUGS, ELECTRON CAPTURE RADIOISOTOPES, HYDROGEN COMPOUNDS, INTERMEDIATE MASS NUCLEI, IODINE ISOTOPES, ISOTOPE APPLICATIONS, ISOTOPES, MAMMALS, MEMBRANES, NERVOUS SYSTEM, NUCLEI, ODD-EVEN NUCLEI, ORGANS, RADIOISOTOPES, RODENTS, SEPARATION PROCESSES, VERTEBRATES
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