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葡萄球菌蛋白 A(简称 SpA)是大多数金黄色葡萄球菌所具有的细胞壁成份,它能与人及多种哺乳动物血清 IgG 的 Fo 片段发生非特异性结合。为进一步研究 SpA 的结构和生物学特性,必须获得纯化的 SpA。纯化方法有用酸沉淀和电泳或用柱层析、凝胶过滤等,但都较繁复,产率不高。Hjelm 等(1972)用溶葡萄球菌素(Lysostaphin)消化细菌后再经 IgG 柱的亲和层析以纯化 SpA,产率高,但溶葡萄球菌素来源困难,价格昂贵。我们利用现有实验条件对这一方法作些改良,获得产率较高的纯化 SpA。
Staphylococcal protein A (SpA) is the cell wall component of most S. aureus and binds nonspecifically to the Fo fragment of human IgG and various mammalian serum IgG. To further study the structural and biological properties of SpA, purified SpA must be obtained. Purification methods useful acid precipitation and electrophoresis or column chromatography, gel filtration, but more complicated, the yield is not high. Hjelm et al. (1972) purify SpA with Lysostaphin after purification by affinity chromatography on IgG column with high yield. Lysostaphin is difficult to source and expensive. We use the existing experimental conditions to make some improvements to this method, to obtain a higher yield of purified SpA.