Affinity chromatography of milk pIgGs on anti-kappa-L-Sepharose.

<p>The chromatography was performed under the conditions of over-saturation of the affinity capacity of the sorbent (A) and re-chromatography of the preparation eluted by acidic buffer (peak 2) on anti-lambda-L-Sepharose (B) under the conditions of the excess of the affinity sorbent. After incubation of a mixture of equal amounts of purified lambda- and kappa-IgGs for 24 h, lambda+kappa-IgG_mix was subjected to standard affinity chromatography on Protein G-Sepharose (C) and gel filtrated (data not shown). Then lambda- and kappa-IgGs were separated by affinity chromatography of lambda+kappa-IgG_mix on anti- lambda-L-Sepharose (D). The preparation of lambda-IgGs purified on anti-lambda-L-Sepharose was rechromatographed on anti-kappa-L-Sepharose (E), while kappa-IgGs on anti-lambda-L-Sepharose (F). In all cases: (–), absorbance at 280 nm (A₂₈₀).