高pH下氨基酰化酶的碱性展开和盐诱导折叠。

Enzyme & protein Pub Date : 1994-01-01 DOI:10.1159/000474993
M Q Huang, H M Zhou
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引用次数: 6

摘要

用荧光光谱、圆二色性光谱和紫外差谱分析了氨基酸酰化酶在碱性条件下展开过程中的构象变化。失活和构象的比较结果表明,使酶分子失活所需的碱性pH值远低于使酶分子发生显著构象变化所需的碱性pH值。当pH值高于12时,虽然酶已失活,但表面上完全展开的酶保留了一些有序的二级结构。在pH为12时,加入KCl,变性酶的相对未展开状态通过疏水坍塌转变为致密构象状态,但没有形成新的二级结构。当pH从12降低到接近中性时,未折叠的酶也发生类似的构象转变。由此可见,疏水塌缩中间体可能是碱性未折叠态到天然态的一般中间构象态。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Alkaline unfolding and salt-induced folding of aminoacylase at high pH.

The conformational changes of aminoacylase during unfolding at alkaline pH have been followed by fluorescence emission, circular dichroism (CD) and ultraviolet difference spectra. The results of comparison of inactivation and conformation show that much lower values of alkaline pH are required to bring about inactivation than significant conformational change of the enzyme molecule. At pH above 12, although the enzyme has been inactivated, the apparently fully unfolded enzyme retains some ordered secondary structure. At pH 12 by adding KCl, the relatively unfolded state of denatured enzyme changes into a compact conformational state by hydrophobic collapsing, but no new secondary structure is formed. On decreasing the pH from pH 12 to approximate neutrality, the unfolded enzyme also undertakes the similar conformational transition. It can be suggested that hydrophobic collapsed intermediate may be a general intermediate conformational state from alkaline unfolded state to native state.

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