Tartary buckwheat 16 kD allergen (TBW16) is located in seed embryo and its biological function is still unknown.Based on the TBW16 sequence obtained from the seed-filling period cDNA library of tartary buckwheat,prokaryotic expression vector pET47b-TBW16 was constructed and TBW16 was successfully overexpressed in E.coli BL21 Star(DE3) in form of inclusion bodies.The TBW16 was renatured by dialysis against gradually decreasing urea solution and further purified by cobalt chelating chromatography.TBW16 was then coupled to Sepharose CL 6B activated by 1,4 butyl glycol two glycidyl ether,and the TBW16 interacting protein was obtained by affinity chromatography protocols.Result of MALDI-TOF mass spectrometry showed that the TBW16 interacting protein has high homology to bacteria porin.This result laid the basis for further revealing the biological functions of TBW16 in tartary buckwheat.