Characteristics of polyamine stimulation of cyclic nucleotide-independent protein kinase reactions.
Characteristics of polyamine stimulation of cyclic nucleotide-independent protein kinase reactions.
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环核苷酸独立蛋白激酶反应的多胺刺激特征。
DOI：
10.1042/bj2320767
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发表时间：
1985
期刊：
影响因子：
--
通讯作者：
Williams-Ashman,HG
中科院分区：
文献类型：
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作者：
Ahmed,K;Goueli,SA;Williams-Ashman,HG
精胺对从肝脏和前列腺纯化的核N1和N2蛋白激酶催化的反应的直接刺激程度关键取决于蛋白底物的性质。化学惰性的Co（NH3）36+离子对蛋白激酶反应的作用类似于亚精胺或精胺。这种增强的磷酸化的各种蛋白质底物的多胺或Co（NH3）63+由纯化的核蛋白激酶制剂进行了研究有关的温度，pH值和其他因素的影响。结果进一步支持了我们的假设[Ahmed，Wilson，Goueli和Williams-Ashman（1978）Biochem.J.176，739-750]，即聚阳离子对某些蛋白激酶反应的增强主要与它们与蛋白底物的相互作用有关，产生更有利于蛋白激酶磷酸化的构象，而不是对其催化活性的直接影响。
The extent of direct stimulation by spermine of reactions catalysed by nuclear N1 and N2 protein kinases purified from liver and prostate depends critically on the nature of the protein substrate. The chemically inert Co(NH3)36+ ion exerts effects on protein kinase reactions similar to those of spermidine or spermine. This enhancement of the phosphorylation of various protein substrates by polyamines or Co(NH3)63+ by purified nuclear protein kinase preparations was studied in relation to effects of temperature, pH and other factors. The results provide further support for our hypothesis [Ahmed, Wilson, Goueli & Williams-Ashman (1978) Biochem. J. 176, 739-750] that the enhancement of certain protein kinase reactions by polycations relates primarily to their interaction with the protein substrate, yielding more favourable conformations for phosphorylation by the protein kinase, rather than a direct effect on its catalytic activity.