Goat immunoglobulin purification on phosphocellulose and deae affigel blue.

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.