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Affinity chromatography of solubilized opioid binding sites using CH-Sepharose modified with a new naltrexone derivative.

Abstract：

:An affinity gel containing a newly synthesized derivative of naltrexone, beta-naltrexyl-6-ethylenediamine (NED), was used to purify opioid binding sites by 300-450-fold. Binding sites solubilized from brains of toad, rat and cow using digitonin in the presence of 0.5 M NaCl are retained by the gel and can be eluted with naloxone (1-3 microM) in yields of 20-25%. The biospecificity of the interaction of opioid binding sites with modified beads is supported by the following: 1) unmodified beads do not retain the binding sites, 2) binding sites prebound with an opioid are not retained, 3) dilution of NED gels with unmodified Sepharose progressively reduced efficiency of retention and 4) specific receptor ligands elute binding sites retained on the NED gels.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Gioannini TL,Howard A,Hiller JM,Simon EJ

doi

10.1016/s0006-291x(84)80295-8

subject

Has Abstract

pub_date

1984-03-15 00:00:00

pages

624-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(84)80295-8

journal_volume

119

pub_type

杂志文章

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