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Urea induced inactivation and unfolding of arginine kinase from the sea cucumber stichopus japonicus

机译：尿素引起的刺参海豚精氨酸激酶失活和解折叠

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摘要

Urea titration was used to study the inactivation and unfolding equilibrium of arginine kinase (AK) from the sea cucumber Stichopus japonicus.Both fluorescence spectral and circular dichroism spectral data indicated that an unfolding intermediate of AK existed in the presence of 1.0 to 2.0 M urea.This was further supported by the results of size exclusion chromatography.The spectral data suggested that this unfolding intermediate shared many structural characteristics with the native form of AK,including its secondary structure,tertiary structure,as well as its quaternary structure.Furthermore,according to the residual activity curve,this unfolding intermediate form still retained its catalytic function although its activity was lower than that of native AK.Taken together,the results of our study give direct evidence that an intermediate with partial activity exists in unfolding equilibrium states of AK during titration with urea.
机译：用尿素滴定法研究了刺参中精氨酸激酶（AK）的失活和解链平衡。荧光光谱和圆二色性光谱数据均表明存在1.0-2.0M尿素时存在AK的解折叠中间体。尺寸排阻色谱的结果进一步证明了这一点。光谱数据表明，这种展开的中间体与AK的天然形式具有许多结构特征，包括其二级结构，三级结构以及四级结构。残留活性曲线表明，这种展开的中间体形式虽然仍比天然AK活性低，但仍保留了其催化功能。综上所述，我们的研究结果直接证明了在分离过程中AK的展开平衡态中存在具有部分活性的中间体。用尿素滴定。

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