Chemical modification of the glycine receptor with fluorescein isothiocyanate specifically affects the interaction of glycine with its binding site.

Abstract:

:Fluorescein 5'-isothiocyanate (FITC) was used to modify lysine residues of the strychnine-sensitive glycine receptor. Pretreatment of rat spinal cord synaptic plasma membranes with FITC specifically affected the ability of glycine to displace [3H]strychnine binding. Glycine completely prevented the effect of FITC modification, suggesting the existence of lysine group(s) either at or in the vicinity of the agonist binding site. Labeling of purified glycine receptor with FITC indicates that such lysine residue(s) are located in the 48,000 daltons polypeptide. Chemical cleavage of the FITC-labeled 48-kilodalton subunit with N-chlorosuccinimide reveals two major labeled fragments of Mr 13.9 kilodalton and 8.5-kilodalton, respectively, the labeling of each being protected by glycine.

authors

Ruiz Gómez A,Fernández-Shaw C,Valdivieso F,Mayor F Jr

doi

10.1016/0006-291x(89)91666-5

subject

Has Abstract

pub_date

1989-04-14 00:00:00

pages

374-81

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(89)91666-5

journal_volume

160

pub_type

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