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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Effects of aspartic acid and potassium chloride on arginine kinase from shrimp
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Effects of aspartic acid and potassium chloride on arginine kinase from shrimp

机译：天门冬氨酸和氯化钾对虾精氨酸激酶的影响

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摘要

The aspartic acid (Asp)-induced unfolding and the salt-induced folding of arginine kinase (AK) were studied in terms of enzyme activity, intrinsic fluorescence emission spectra, 1-anilino-8-naphthalenesulfonate (ANS) fluorescence spectra and far-UV circular dichroism (CD) spectra. The results showed that Asp caused inactivation and unfolding of AK with no aggregation during AK denaturation. The unfolding of the whole molecule and the inactivation of AK in different Asp concentrations were compared. Much lower Asp concentration was required to induce inactivation than to produce significant conformational changes of the enzyme molecule. However, with further addition of Asp, the molar ellipticity at 222 and 208 nm, the wavelength shift and the emission intensity of ANS hardly changed. Asp denatured AK was reactivated by dilution. In addition, potassium chloride (KCl) induced the molten globule state with a compact structure after AK was denatured with 7.5 mM Asp. These results collectively elucidate the osmotic effect of Asp anions for the molten globule formed during unfolding process. They also suggest that the effect of Asp differed from that of other denaturants such as guanidine hydrochloride or urea during AK folding. The molten globule state indicates that intermediates exist during AK folding. (c) 2006 Elsevier B.V. All rights reserved.
机译：从酶活性，固有荧光发射光谱，1-苯胺基-8-萘磺酸盐（ANS）荧光光谱和远紫外光谱方面研究了天冬氨酸（Asp）诱导的解折叠和盐诱导的精氨酸激酶（AK）的折叠。圆二色性（CD）光谱。结果表明，Asp导致AK变性过程中AK失活和展开，没有聚集。比较了整个分子的展开和不同Asp浓度下AK的失活。诱导灭活所需的Asp浓度要比产生酶分子的显着构象变化低得多。然而，随着Asp的进一步添加，在222和208nm处的摩尔椭圆率，ANS的波长偏移和发射强度几乎不变。通过稀释将Asp变性的AK重新活化。此外，在用7.5 mM Asp使AK变性后，氯化钾（KCl）诱导了具有致密结构的熔融球状状态。这些结果共同阐明了Asp阴离子对展开过程中形成的熔融小球的渗透作用。他们还表明，在AK折叠过程中，Asp的作用与其他变性剂（如盐酸胍或尿素）不同。熔融小球状态表明在AK折叠过程中存在中间体。 （c）2006 Elsevier B.V.保留所有权利。

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