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多胺对不依赖环核苷酸的蛋白激酶反应的刺激特性。

Characteristics of polyamine stimulation of cyclic nucleotide-independent protein kinase reactions.

作者信息

Ahmed K, Goueli S A, Williams-Ashman H G

出版信息

Biochem J. 1985 Dec 15;232(3):767-71. doi: 10.1042/bj2320767.

Abstract

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.

摘要

从肝脏和前列腺中纯化得到的核N1和N2蛋白激酶所催化的反应,精胺对其直接刺激的程度关键取决于蛋白质底物的性质。化学性质惰性的Co(NH3)36+离子对蛋白激酶反应产生的效应,与亚精胺或精胺的效应相似。通过纯化的核蛋白激酶制剂,研究了多胺或Co(NH3)63+对各种蛋白质底物磷酸化的这种增强作用与温度、pH及其他因素的效应之间的关系。这些结果为我们的假说[Ahmed、Wilson、Goueli和Williams-Ashman(1978年)《生物化学杂志》176, 739 - 750]提供了进一步的支持,即多阳离子对某些蛋白激酶反应的增强作用主要与其与蛋白质底物的相互作用有关,从而产生更有利于蛋白激酶进行磷酸化的构象,而非对其催化活性的直接影响。

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Interaction of polyamines and magnesium with casein kinase II.多胺和镁与酪蛋白激酶II的相互作用。
Arch Biochem Biophys. 1984 Aug 15;233(1):133-8. doi: 10.1016/0003-9861(84)90609-x.

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