The effect of monovalent ions on polyphosphate binding to Escherichia coli exopolyphosphatase.
The effect of monovalent ions on polyphosphate binding to Escherichia coli exopolyphosphatase.
复制标题
单价离子对多磷酸盐与大肠杆菌外多磷酸酶结合的影响。
DOI：
10.1006/bbrc.2000.3128
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
Keasling,JD
中科院分区：
文献类型：
--
作者：
Bolesch,DG;Keasling,JD
研究了大肠杆菌外切多聚磷酸酶（PPX）与多聚磷酸盐相互作用的热力学驱动力。这种相互作用被认为是阳离子浓度无关，但弱依赖于某些阴离子的浓度。这两种特征对于非特异性蛋白质-酶相互作用来说都是非常罕见的。这些结果的解释的基础上的理论表明，结合不是熵驱动的，由于聚电解质凝聚的抗衡离子的释放，几乎所有的蛋白质的相互作用的情况下。PPX-聚磷酸盐相互作用的热力学仅与多核苷酸与单链结合蛋白的相互作用相似。
The thermodynamic driving force for the interaction of Escherichia coli exopolyphosphatase (PPX) with polyphosphate was investigated by varying salt choice and concentration. This interaction was found to be cation concentration independent but weakly dependent on the concentration of certain anions. Both of these traits are very uncommon for nonspecific protein–polyelectrolyte interactions. Interpretation of these results based on theory indicated that binding was not entropy driven due to release of polyelectrolyte-condensed counterions, as is the case for nearly all protein–polyelectrolyte interactions. The thermodynamics of the PPX–polyphosphate interaction showed similarity only to the interaction of polynucleotides with single stranded binding proteins.