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000837812 1001_ $$0P:(DE-Juel1)131989$$aYang, Ge$$b0$$ufzj
000837812 245__ $$aExpression, purification, and preliminary characterization of human presenilin-2
000837812 260__ $$aAmsterdam [u.a.]$$bElsevier Science$$c2018
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000837812 520__ $$aPresenilins (PS1 and PS2) exhibit similar γ-secretase-dependent and −independent functions with subtle variations. In this study, we established a cost-effective process to overexpress and purify full-length human PS2 in sufficient quantities and quality for structural studies. Upon optimization, milligram quantities of homogeneous trimeric hisPS2 were purified, which enabled the preliminary characterization of human hisPS2 zymogen. Far-UV and near-UV CD as well as fluorescence spectroscopy revealed that purified hisPS2 contained the expected secondary structure and was folded into a defined tertiary structure. Thermal stability analysis revealed a Tm value of ∼55 °C for secondary structure while cholesterol significantly increased the stability. The low melting temperature of ∼34 °C for the tertiary structure was able to explain the purity and aggregation problems observed during purification. Additionally, the occurrence of calcium ions induced structural changes to different extents for PS2WT and PS2-D263A/D366A was observed, which is consistent with previous studies.
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000837812 7001_ $$0P:(DE-HGF)0$$aYu, Kun$$b1
000837812 7001_ $$0P:(DE-HGF)0$$aKubicek, Jan$$b2
000837812 7001_ $$0P:(DE-Juel1)131973$$aLabahn, Jörg$$b3$$eCorresponding author$$ufzj
000837812 773__ $$0PERI:(DE-600)2016483-X$$a10.1016/j.procbio.2017.09.012$$gp. S1359511317300065$$p63-73$$tProcess biochemistry$$v64$$x1359-5113$$y2018
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