We describe a method for the efficient purification of immunoglobulins G (IgG)to near homogeneity from goat serum. This was achieved by performing first an AS-40 fractionation on goat serum, followed by chromatography on phosphocellulose (P11) equilibrated in citrate buffer at pH 5.7. Peak I, eluted at V0from P11, contained all IgG and the other serum proteins,except β -globulins and most of the a -2- globulins, which are eluted in a second peak with 0.24 M K-phosphate in citrate buffer at pH 6.0. Peak I, concentrated and dialyzed in 20 mM K-phosphate buffer pH 8.0, was then applied onto a DEAE Affi-Gel Blue column equilibrated in the same buffer. Two peaks were obtained from this column: peak I, eluted at V0contained a pure IgG fraction,while the other serum proteins were in peak II.We conclude that the P11 step performed under the conditions we report here,is very useful to retain the α- 2 and β-globulins, which contaminate the IgG when only the DEAE Affi-Gel Blue purification step is used.
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