Isolation and purification of morphine receptor by affinity chromatography

Tae Mook Cho, Bang Lun Ge, Horace H. Loh

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Brain membranes were solubilized by sonication and Triton X-100 extraction and applied to an affinity column consisting of a 6-succinyl morphine derivative of Affi Gel-102. A fraction exhibiting high opiate binding was eluted by tris-buffer containing naloxone, CHAPS and NaCl. This fraction consisted of both proteins and acidic lipids. The opiate binding properties of this purified material exhibited many properties similar to those of membrane bound receptors of the u-type, including high affinity, stereospecificity, Na-effect and rank order in affinity for opiates. This opiate binding material was highly sensitive to both trypsin and N-ethylmaleimide. Based on the protein content of the isolated membrane receptor, a 3200-fold purification over the original brain P2 fraction was achieved.

Original languageEnglish (US)
Pages (from-to)1075-1085
Number of pages11
JournalLife Sciences
Volume36
Issue number11
DOIs
StatePublished - Mar 18 1985

Bibliographical note

Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.

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