Purification to apparent homogeneity of a μ-type opioid receptor from rat brain

T. M. Cho, J. I. Hasegawa, B. L. Ge, H. H. Loh

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Abstract

A μ-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 M(r) 58,000 value agrees closely with that determined by covalently labeling purified receptor with bromoacetyl-[3H]dihydromorphine or with125I-labeled β-endorphin and dimethyl suberimidate.

Original languageEnglish (US)
Pages (from-to)4138-4142
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume83
Issue number12
DOIs
StatePublished - 1986

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