Phosphorylation of gamma-aminobutyrate (GABA)/benzodiazepine receptors by cyclic AMP-dependent protein kinase.
Phosphorylation of gamma-aminobutyrate (GABA)/benzodiazepine receptors by cyclic AMP-dependent protein kinase.
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环 AMP 依赖性蛋白激酶对 γ-氨基丁酸 (GABA)/苯二氮卓受体进行磷酸化。
DOI:
10.1042/bj2590613
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发表时间:
1989
期刊:
影响因子:
--
通讯作者:
Turner,AJ
中科院分区:
文献类型:
--
作者:
Kirkness,EF;Bovenkerk,CF;Ueda,T;Turner,AJ
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.