Quantitative analysis of dissociation of LDH by high pressure native PAGE
Quantitative analysis of dissociation of LDH by high pressure native PAGE
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高压非变性 PAGE 定量分析 LDH 解离
DOI：
10.1080/08957959.2018.1564822
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发表时间：
2019
影响因子：
2
通讯作者：
Fujisawa Tetsuro
中科院分区：
文献类型：
--
作者：
Miwa Tomoya;Ishiguro Ryo;Kameyama Keiichi;Fujisawa Tetsuro
高压天然聚丙烯酰胺凝胶电泳已被设计用于可视化蛋白质复合物的解离/结合过程。本文以猪心脏乳酸脱氢酶（一种四聚体蛋白）的压力解离为例，对该方法进行了更定量的研究。在压力达到150mpa时，我们观察了电泳图谱的变化。通过优化缓冲系统和对染色凝胶进行仔细的图像分析，我们定量了加压过程中的所有解离物。我们通过与先前报道的结果进行比较，讨论了我们的方法的特点。
High pressure native polyacrylamide gel electrophoresis has been designed to visualize the dissociation/association process of protein complexes. This paper reports this methodology in more quantitative way by inspecting pressure dissociation of pig heart lactate dehydrogenase, a tetrameric protein, which was extensively investigated in spectroscopic methods. We observed the change of electrophoresis pattern with pressure up to 150 MPa. By optimizing the buffer system and careful image analysis of the stained gels, we quantified all the dissociates in the process of pressurization. We discussed the characteristics of our methodology by comparing the result with the previously reported.