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Literature DB >> 2541695

Phosphorylation of gamma-aminobutyrate (GABA)/benzodiazepine receptors by cyclic AMP-dependent protein kinase.

E F Kirkness¹, C F Bovenkerk, T Ueda, A J Turner.

Abstract

Preparations of gamma-aminobutyrate (GABA)/benzodiazepine receptor from pig cerebral cortex are composed of three major bands of polypeptides (51, 55 and 57 kDa) which are purified in a ratio of approx. 2:1:1 respectively. Treatment of purified receptor preparations with cyclic AMP-dependent protein kinase resulted in major incorporation of 32P into the 55 kDa band only. The maximum incorporation achieved was 0.6 mol of 32P/mol of 55 kDa polypeptide. The phosphorylated receptor subunit (beta-subunit) displays the same apparent Mr as a band labelled irreversibly with the GABA receptor agonist [3H]muscimol. The two nonphosphorylated subunit polypeptides (51 and 57 kDa) are each labelled irreversibly with [3H]flunitrazepam and are recognized by anti-peptide antibodies specific for alpha-subunits.

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Year: 1989 PMID： 2541695 PMCID： PMC1138555 DOI： 10.1042/bj2590613

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

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