通过钙亲和层析法纯化人血清淀粉样蛋白P成分（SAP）。
Purification of human serum amyloid P component (SAP) by calcium affinity chromatography.
作者信息
Mantovaara T, Pertoft H, Porath J
机构信息
Institute of Biochemistry, University of Uppsala, Sweden.
出版信息
Biotechnol Appl Biochem. 1989 Dec;11(6):564-70.
Serum amyloid P component (SAP) has been purified from human serum by means of immobilized metal ion affinity chromatography (IMAC). It was selectively concentrated on carboxymethylated aspartic acid agarose (CM-Asp-agarose) loaded with calcium and, employing very mild conditions, purified to electrophoretical and immunological homogeneity in a single step amounting to about 1900-fold purification. As a purification method our procedure thus compares well with bio-specific affinity chromatography.
血清淀粉样蛋白P成分（SAP）已通过固定化金属离子亲和色谱法（IMAC）从人血清中纯化出来。它被选择性地浓缩在负载钙的羧甲基化天冬氨酸琼脂糖（CM-Asp-琼脂糖）上，并在非常温和的条件下，一步纯化至电泳和免疫均一性，纯化倍数约为1900倍。因此，作为一种纯化方法，我们的程序与生物特异性亲和色谱法相比效果良好。
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