Berger D, Beger H G
Clin Chim Acta. 1987 Mar 30;163(3):289-99. doi: 10.1016/0009-8981(87)90247-6.
In the present paper the ability of Gc-globulin and transferrin to bind endotoxin of Escherichia coli 0 111: B 4 is demonstrated. This conclusion is based on four lines of evidence. By affinity chromatography using lipopolysaccharide of E. coli 0 111: B 4 two endotoxin-binding proteins of serum were identified, showing an apparent molecular weight of 77,000 and 51,000, respectively. If serum samples preincubated with the tritiated endotoxin form have undergone isoelectric focusing under non-denaturing conditions one radioactive peak appears which coincides with the precipitate obtained by immunoelectrophoresis against anti-human Gc-globulin and anti-human transferrin. Radioimmunoprecipitation experiments of serum showed that tritiated endotoxin of E. coli 0 111: B 4 was only found in the precipitate obtained with anti-Gc-globulin, antitransferrin, and polyvalent antiserum against human serum. By isoelectric focusing of purified proteins 3H-lipopolysaccharide of E. coli 0 111: B 4 was only found associated with human Gc-globulin and transferrin.
本文证明了Gc球蛋白和转铁蛋白结合大肠杆菌0111:B4内毒素的能力。这一结论基于四条证据。通过使用大肠杆菌0111:B4的脂多糖进行亲和层析，鉴定出了血清中的两种内毒素结合蛋白，其表观分子量分别为77,000和51,000。如果将预先与氚标记的内毒素形式孵育的血清样品在非变性条件下进行等电聚焦，会出现一个放射性峰，该峰与用抗人Gc球蛋白和抗人转铁蛋白进行免疫电泳得到的沉淀相重合。血清的放射免疫沉淀实验表明，大肠杆菌0111:B4的氚标记内毒素仅在使用抗Gc球蛋白、抗转铁蛋白和抗人血清多价抗血清获得的沉淀中发现。通过对纯化蛋白进行等电聚焦，发现大肠杆菌0111:B4的3H-脂多糖仅与人Gc球蛋白和转铁蛋白相关。
