Chemical modification of opiate receptors with ethoxyformic anhydride and photo-oxidation: Evidence for essential histidyl residues

Roy, B.P.; Ng, Andrew Y.

doi:10.1016/0006-291x(82)91752-1

Biochemical and Biophysical Research Communications

1982

DOI: 10.1016/0006-291x(82)91752-1

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Chemical modification of opiate receptors with ethoxyformic anhydride and photo-oxidation: Evidence for essential histidyl residues

B.P. Roy

Andrew Y. Ng

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Cited by 8 publications

(1 citation statement)

References 21 publications

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“…Experimental modification of opioid receptors with site-specific reagents has provided significant information on chemical structure essential to receptor functions. For example, the presence of functional histidyl residues in opioid receptors from rat brain has been demonstrated by modification of opioid receptors using a histidyl-specific reagent, ethoxyformic anhydride (Roy and Ng, 1982). The implication of sulfhydryl (SH) residues in ligand-binding activity has been shown by several experiments using SHmodifying reagents such as N-ethylmaleimide (NEM) (Simon and Groth, 1975;Wilson et al, 1975), iodoacetamide , and 5,5'-dithiobis-(2nitrobenzoic acid) Nozaki and Cho, 1985).…”

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confidence: 99%

Evidence for Disulfide Bonds in Membrane‐Bound and Solubilized Opioid Receptors

Kamikubo

Murase

Murayama

et al. 1988

Journal of Neurochemistry

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The effects of pretreatment with dithiothreitol (DTT) on opioid binding activities of membrane-bound and digitonin-solubilized opioid receptors from bovine adrenal medulla were studied. Pretreatment of membranes with DTT or mercaptoethanol inhibited [3H]diprenorphine binding by reducing the number of binding sites. The inhibitory action of DTT was time and dose dependent. The binding of [3H]D-Ala2-D-Leu5-enkephalin was also inhibited by DTT pretreatment. Pretreatment of digitonin-solubilized binding sites with DTT also reduced the number of [3H]diprenorphine binding sites. The action of DTT was diminished by preincubating the DTT solution with H2O2. [3H]Diprenorphine protected the opioid binding sites from the inhibitory action of DTT. The present results provide evidence that disulfide bonds are implicated in opioid binding activity of the opioid receptor system.

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mentioning

confidence: 99%

Evidence for Disulfide Bonds in Membrane‐Bound and Solubilized Opioid Receptors

Kamikubo

Murase

Murayama

et al. 1988

Journal of Neurochemistry

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The chemistry of the opioid receptor binding sites

Medzihradszky

2003

Journal of Peptide Science

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Since the discovery of the opioid receptors and their endogenous ligands an immense research work has been devoted to the exploration of their specificity, the mechanism of ligand binding and ligand-receptor interactions. One of the main goals has been the location and characterization of the binding sites. The present review compiles the results achieved in this field in the last quarter of a century, and puts some questions concerning the success of these efforts.

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Modification of rat liver iodothyronine 5′-deiodinase activity with diethylpyrocarbonate and Rose Bengal; Evidence for an active site histidine residue

Mol¹,

Docter²,

Hennemann³

et al. 1984

Biochemical and Biophysical Research Communications

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Chemical modification of opiate receptors with ethoxyformic anhydride and photo-oxidation: Evidence for essential histidyl residues

Cited by 8 publications

References 21 publications

Evidence for Disulfide Bonds in Membrane‐Bound and Solubilized Opioid Receptors

Evidence for Disulfide Bonds in Membrane‐Bound and Solubilized Opioid Receptors

The chemistry of the opioid receptor binding sites

Modification of rat liver iodothyronine 5′-deiodinase activity with diethylpyrocarbonate and Rose Bengal; Evidence for an active site histidine residue

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