Objective To evaluate the procedures to purify IgG with simple and rapid,high purity and high biological activity from Paguma larvate serum. Methods The Paguma larvate serum IgG was purified by Hitrap Protein A affinity chromatography and 8% non-reduced SDS-PAGE. The purity was identified by 12% SDS-PAGE, and compared the method on purification of IgG from Paguma larvate serum. The purification efficiency of the two methods was compared by amino black staining and protein A-HRP blotting. Results The IgG purified from Protein A affinity chromatography showed a high protein A- HRP binding activity, but purity is lower than non-reduced SDS-PAGE and the IgG from non-reduced SDS-PAGE also showed same levels of protein A-HRP binding activity. Conclusion For Paguma larvate serum IgG, purification by 8% non-reduced SDS-PAGE is an ideal method.