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用六聚体肽配基通过亲和层析从 Cohn 级分 II+III、脱脂乳和乳清中纯化多克隆抗体。

Purification of polyclonal antibodies from Cohn fraction II + III, skim milk, and whey by affinity chromatography using a hexamer peptide ligand.

机构信息

Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695-7905, USA.

出版信息

J Sep Sci. 2012 Nov;35(22):3139-48. doi: 10.1002/jssc.201200199. Epub 2012 Jul 2.

Abstract

HWRGWV, a peptide that binds specifically to the Fc fragment of human immunoglobulin G (IgG), was used for the purification of IgG from Cohn fraction II + III of human plasma and from bovine skim milk and whey. The concentration of sodium chloride and sodium caprylate in the binding buffer as well as the pH of the elution buffer were optimized to achieve high IgG yield and purity. Under optimized conditions, IgG was recovered from plasma fractions with yield and purity up to 84% and 95%, respectively. IgG was also purified from skim milk with 74% yield and 92% purity and from whey with 85% yield and 93% purity. Purification experiments were also performed with Protein A resin and the results were found to be similar to those obtained with the peptide adsorbent.

摘要

HWRGWV 是一种与人类免疫球蛋白 G(IgG)的 Fc 片段特异性结合的肽,用于从人血浆的 Cohn 级分 II+III 和牛脱脂乳及乳清中纯化 IgG。结合缓冲液中氯化钠和辛酸钠的浓度以及洗脱缓冲液的 pH 值都经过了优化,以达到高 IgG 产率和纯度。在优化条件下,IgG 从血浆级分中的回收率分别高达 84%和 95%。IgG 也可从脱脂乳中以 74%的产率和 92%的纯度、从乳清中以 85%的产率和 93%的纯度进行纯化。还使用 Protein A 树脂进行了纯化实验,结果与使用肽吸附剂得到的结果相似。

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