Purification of human C‐reactive protein by barium sulfate and preparative agarose electrophoresis
Purification of human C‐reactive protein by barium sulfate and preparative agarose electrophoresis
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DOI：
10.1111/j.1699-0463.1989.tb00494.x
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发表时间：
1989-07
期刊：
影响因子：
2.8
通讯作者：
C. Kindmark;Jim C. Williams
中科院分区：
文献类型：
--
作者：
C. Kindmark;Jim C. Williams
描述了从人血清中纯化C反应蛋白（CRP）的方法。所描述的方法利用CRP的硫酸钡吸附特性和在含有Ca2+的琼脂糖凝胶中电泳期间CRP迁移的独特生物物理特性。通过SDS聚丙烯酰胺凝胶电泳过程中还原蛋白的迁移测定，纯化的CRP具有28，000的表观分子量。所描述的方法具有不需要分子筛或亲和色谱法从人血清中纯化同质CRP的优点。
A procedure is described for the purification of C‐reactive protein (CRP) from human serum. The methods described take advantage of the barium sulfate adsorption property of CRP and the unique biophysical property of CRP migration during electrophoresis in agarose gels containing Ca2+. The purified CRP had an apparant molecular weight of 28,000 as determined by migration of the reduced protein during SDS polyacrylamide gel electrophoresis. The described procedure has the advantage of not requiring either molecular sieve or affinity chromatography for purification of homogenous CRP from human sera.