一种用于快速高效洗脱天然亲和纯化的蛋白A标签复合物的方法。
A method for the rapid and efficient elution of native affinity-purified protein A tagged complexes.
作者信息
Strambio-de-Castillia Caterina, Tetenbaum-Novatt Jaclyn, Imai Brian S, Chait Brian T, Rout Michael P
机构信息
Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, NY 10021-6399, USA.
出版信息
J Proteome Res. 2005 Nov-Dec;4(6):2250-6. doi: 10.1021/pr0501517.
A problem faced in proteomics studies is the recovery of tagged protein complexes in their native and active form. Here we describe a peptide, Bio-Ox, that mimics the immunoglobulin G (IgG) binding interface of Staphylococcus aureus Protein A, and competitively displaces affinity-purified Protein A fusion proteins and protein complexes from IgG-Sepharose. We show that Bio-Ox elution is a robust method for the efficient and rapid recovery of native tagged proteins, and can be applied to a variety of structural genomics and proteomics studies.
蛋白质组学研究中面临的一个问题是如何以天然和活性形式回收标记的蛋白质复合物。在此，我们描述了一种名为Bio-Ox的肽，它模拟了金黄色葡萄球菌蛋白A的免疫球蛋白G（IgG）结合界面，并能竞争性地从IgG-琼脂糖凝胶上置换出亲和纯化的蛋白A融合蛋白和蛋白质复合物。我们表明，Bio-Ox洗脱是一种高效、快速回收天然标记蛋白的可靠方法，可应用于各种结构基因组学和蛋白质组学研究。
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