Chuang C Y, Wang W P, Luo S F, Lin K T, Chen C Y, Chen W Y
Zhonghua Min Guo Wei Sheng Wu Ji Mian Yi Xue Za Zhi. 1980 Sep;13(3):287-92.
Three myeloma proteins, IgG lambda, IgA lambda and IgM lambda, were identified by protein electrophoresis (PEP), immunoglobulin quantitation and immunoelectrophoresis (IEP). Preparative block electrophoresis was generally carried out as an initial step to separate the myeloma proteins. The myeloma proteins thus separated were then passed through either diethylaminoethyl (DEAE) ion exchange chromatography and recycled in a Sephadex G-200 column, or first through gel filtration and recycled in DEAE. An attempt to bypass the step of preparative electrophoresis in the separation of IgG myeloma protein by passing the serum directly into a DEAE column was proved to be inappropriate. The IgM myeloma protein had a marked tendency to cryoprecipitate and to form euglobulin, and this property was utilized to separate the crude myeloma protein. The purified myeloma protein fractions were concentrated and dialyzed with Ultrafiltration (Amicon) and retested for purity with PEP, double diffusion (DD) and IEP. Some special physiochemical properties which affected the purification procedures are discussed.
通过蛋白质电泳（PEP）、免疫球蛋白定量和免疫电泳（IEP）鉴定出三种骨髓瘤蛋白，即IgG λ、IgA λ和IgM λ。制备性区带电泳通常作为分离骨髓瘤蛋白的第一步。然后，将如此分离出的骨髓瘤蛋白通过二乙氨基乙基（DEAE）离子交换色谱，再在葡聚糖凝胶G - 200柱中循环，或者先通过凝胶过滤，再在DEAE中循环。尝试通过将血清直接注入DEAE柱来绕过制备性电泳步骤以分离IgG骨髓瘤蛋白，结果证明是不合适的。IgM骨髓瘤蛋白有明显的冷沉淀和形成优球蛋白的倾向，利用这一特性来分离粗制的骨髓瘤蛋白。纯化的骨髓瘤蛋白组分通过超滤（Amicon）进行浓缩和透析，并用PEP、双向扩散（DD）和IEP重新检测纯度。讨论了一些影响纯化过程的特殊理化性质。
