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One-Step Affinity Purification of Human Mu-Opioid Receptor Overexpressed in Baculovirus System

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Affinity chromatography on Ni-nitrilotriacetic acid agarose was used to purify human mu-opioid receptors overexpressed in Sf9 cells. We introduced a tag of 6 consecutive histidines at its carboxyl terminus for easy purification of recombinant proteins. The binding activity and identification of the purified receptor were determined by receptor binding assay, SDS-PAGE and Western blotting analysis. This procedure used in the paper offer an easy and fast route to the purification of recombinant human mu-opioid receptors.
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Keywords: BACULOVIRUS; Receptor binding assay; Spodoptera frugiperda; Trichoplusia ni; opioid receptor (MOR)

Document Type: Review Article

Publication date: 2001-08-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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