Habeeb A F, Francis R D
Vox Sang. 1977;32(3):143-58. doi: 10.1111/j.1423-0410.1977.tb00619.x.
Human IgG separated by Cohn fractionation showed variability in the content of aggregates, plasminogen and anticomplement activity. The plasminogen was removed or markedly reduced by affinity chromatography on Sepharose-lysine. Anticomplement activity was reduced by chromatography of Cohn fraction II on DEAE-cellulose. Preparations of IgG obtained by chromatography of intermediates from Cohn fractionation (e.g. Cohn FII + FIII or FII + FIII W) on DEAE-cellulose were devoid of aggregates, plasminogen and exhibited reduced anticomplement activity. The initial levels of specific antibody activity to viral agents were recovered in the IgG fractions. Fragmentation of IgG during storage was prevented or greatly reduced by removal of plasminogen by affinity chromatography on Sepharose-lysine.
通过科恩分级分离法分离得到的人免疫球蛋白G（Human IgG）在聚集体含量、纤溶酶原和抗补体活性方面表现出变异性。通过赖氨酸琼脂糖亲和层析可去除或显著降低纤溶酶原。通过在二乙氨基乙基纤维素（DEAE - cellulose）上对科恩分级分离II级分进行层析，可降低抗补体活性。通过对科恩分级分离中间产物（如科恩FII + FIII或FII + FIII W）在二乙氨基乙基纤维素上进行层析获得的免疫球蛋白G制剂不含聚集体、纤溶酶原，且抗补体活性降低。在免疫球蛋白G级分中恢复了针对病毒制剂的特异性抗体活性的初始水平。通过赖氨酸琼脂糖亲和层析去除纤溶酶原，可防止或大大减少免疫球蛋白G在储存期间的片段化。
