Immunology Section, Indian Veterinary Research Institute, Izatnagar-243122 (UP) India.
A simple, two-step procedure to purify the immunoglobulin G (IgG) fraction from mouse sera is described. The rationale for the procedure is, firstly, to precipitate the mouse serum with ammonium sulphate and secondly, to subject the precipitate to ion exchange chromatography with DE-52 column. DE-52 chromatography following ammonium sulphate precipitation was found to be a quite satisfactory method for the reasonable purification of mouse immunoglobulin (IgG) as observed in SDS-PAGE. Thereafter, the optimum condition for digestion of mouse IgG with papain has been standardized. The controlled digestion procedure followed for the cleavage of the immunoglobulin in the present study was quite significant and yielded a 25, 55 and 110 kDa peptide which were represented as Fc, Fab and F(ab)2 fragments, respectively.
Ammonium sulphate, DE-52, mouse, immunoglobulin, serum, papain
