Adenosine-3',5'-monophosphate-dependent protein kinase from bovine anterior pituitary gland. 3. Structural specificity of the ATP site of the catalytic subunit.
Adenosine-3',5'-monophosphate-dependent protein kinase from bovine anterior pituitary gland. 3. Structural specificity of the ATP site of the catalytic subunit.
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来自牛垂体前叶的腺苷-3,5-单磷酸依赖性蛋白激酶。
DOI:
10.1139/o74-021
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发表时间:
1974
期刊:
影响因子:
--
通讯作者:
M. Gauthier
中科院分区:
文献类型:
--
作者:
S. Lemaire;F. Labrie;M. Gauthier
The effect of analogues and derivatives of adenosine 3′,5′-monophosphate (cyclic AMP) and of ATP on the incorporation of 32P from [γ-32P]ATP into histones has been measured using the purified catalytic subunit of adenohypophyseal protein kinase. Gamma-labeled CTP, GTP, and UTP cannot substitute for [γ-32P]ATP but they slightly inhibit the phosphorylation by [γ-32P]-ATP when present as unlabeled compounds. A stringent requirement of the adenine nucleus is observed for the ability to compete at the ATP site, inhibitions of 42, 39, 32, and 63% being observed respectively with adenine, adenosine, 5′AMP, and ADP, while the corresponding purine or pyrimidine derivatives have no effect when present at a 13-fold molar excess relative to [γ-32P]ATP. The N6-benzoyl and N6-butyryl derivatives of cyclic AMP are inactive whereas the 8-substituted derivatives are generally as active as cyclic AMP itself, except for the 8-amino- and 8-hydroxy-derivatives, which exhibit a lower degree of competition. All cyclic AMP and A...