Skobel'tsyna L M, Ermolaev V I, Skripkina L A, Romashenko A G
Biokhimiia. 1991 Sep;56(9):1688-700.
A procedure for large-scale separation and purification of two mink serum macroglobulins, Lpm and alpha 2M, is described. Individual preparations of each of these macroglobulins were obtained in an immunologically pure state. After precipitation from the serum at 6.5-13% PEG 6000, Lpm and alpha 2M were separated by a pH stepwise gradient elution metal chelate affinity chromatography and purified by chromatographies on Biogel A 1.5 m and DEAE-Trisacryl M. Each of these macroglobulins was tested by counter-immunoelectrophoresis with the corresponding monospecific antiserum. The yields per 100 ml of the source serum were 23-44 mg of Lpm and 7-30 mg of alpha 2M which corresponded to 10-20% of their serum contents. Some of general biochemical properties of mink Lpm and alpha 2M and of all mammalian alpha-macroglobulins are discussed.
本文描述了一种大规模分离和纯化两种水貂血清巨球蛋白(Lpm和α2M)的方法。每种巨球蛋白的单独制剂均以免疫纯态获得。在6.5 - 13%聚乙二醇6000(PEG 6000)存在下从血清中沉淀后,通过pH梯度洗脱金属螯合亲和色谱法分离Lpm和α2M,并通过在Biogel A 1.5 m和DEAE - Trisacryl M上的色谱法进行纯化。用相应的单特异性抗血清通过对流免疫电泳对每种巨球蛋白进行检测。每100 ml源血清中Lpm的产量为23 - 44 mg,α2M的产量为7 - 30 mg,分别相当于其血清含量的10 - 20%。文中还讨论了水貂Lpm和α2M以及所有哺乳动物α - 巨球蛋白的一些一般生化特性。