Purification to apparent homogeneity of a mu-type opioid receptor from rat brain.
A mu-opioid-specific receptor was purified to apparent homogeneity from rat brain membranes by 6-succinylmorphine affinity chromatography, gel filtration, wheat germ agglutinin affinity chromatography, and isoelectric focusing. The purified receptor had a molecular weight of 58,000 as determined by NaDodSO4/polyacrylamide gel electrophoresis and was judged to be homogeneous by the following criteria: (i) a single band was detected by autoradiography after NaDodSO4/polyacrylamide gel electrophoresis of 125I-labeled receptor and (ii) the purified preparation had a specific opioid-binding activity of 17,720 pmol/mg of protein, close to the theoretical value. In addition, the Mr 58,000 value agrees closely with that determined by covalently labeling purified receptor with bromoacetyl-[3H]dihydromorphine or with 125I-labeled beta-endorphin and dimethyl suberimidate.
D000818:Animals; D001923:Brain Chemistry; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004174:Diprenorphine / Q000378:metabolism; D004723:Endorphins / Q000378:metabolism; D007525:Isoelectric Focusing; D008970:Molecular Weight; D051381:Rats; D011957:Receptors, Opioid / Q000302:isolation & purification* / Q000378:metabolism; D017450:Receptors, Opioid, mu; D001615:beta-Endorphin
D004723:Endorphins; D011957:Receptors, Opioid; D017450:Receptors, Opioid, mu; D004174:Diprenorphine; D001615:beta-Endorphin