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Ammonium sulfate
Company: Carl Roth
Catalog#: 3746.1
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Quantitative Determination of Ca2+-binding to Ca2+-sensor Proteins by Isothermal Titration Calorimetry
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2020-04-05
[Abstract]  Diverse and complex molecular recognitions are central elements of signal transduction cascades. The strength and nature of these interaction modes can be determined by different experimental approaches. Among those, Isothermal titration calorimetry (ITC) offers certain advantages by providing binding constants and thermodynamic parameters from titration series without a need to label or immobilize one or more interaction partners. Furthermore, second messenger homeostasis involving Ca2+-ions requires in particular knowledge about stoichiometries and affinities of Ca2+-binding to Ca2+-sensor proteins or Ca2+-dependent regulators, which can be obtained by employing ITC. We used ITC to measure these parameters for a set of neuronal Ca2+-sensor ... [摘要]  [摘要] 多样而复杂的分子识别是信号转导级联的核心要素。这些相互作用模式的强度和性质可以通过不同的实验方法来确定。其中，等温滴定热量法（ITC）通过提供来自滴定系列的结合常数和热力学参数，而无需标记或固定一个或多个相互作用伙伴，从而提供了某些优势。此外，涉及钙第二信使动态平衡2+ -离子需要小号特别知识大约化学计量和Ca的亲和力2+ -结合对于Ca 2+ 多个传感器蛋白或钙2+ 依赖的调节器，可以通过使用ITC获得。我们使用ITC来测量在感光细胞中运行的一组神经元Ca 2+ 传感器蛋白的这些参数。在这里，我们提出了一个分步协议，以（a）测量与Ca 2+ 传感器鸟苷酸环化酶e激活蛋白1的Ca 2+ 相互作用，（b）设计ITC实验并准备样品，（c）去除Ca 2+ 几乎完全来自Ca 2+ 结合蛋白，而无需使用螯合剂（如EGTA）。

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