Abstract:Parvalbumin is the major allergen of fish species. The different subtypes of salmon parvalbumin with close molecular weight and sequence bring great challenges to protein separation and purification. Parvalbu－ minβ1 was purified by heat treatment，（NH4）2SO4 salting out method and Qxl-Sepharose chromatography com－ bined by gel filtration. Western blotting was used to identify the allergenicity of purified Parvalbumin. MALDITOF/MS was used to further identify the characteristic of parvalbumin structure. The results revealed that the purity of the parvalbumin β1 was more than 90 percent and it had immunological reactive activity. Investigation into this protein is beneficial not only to detecting allergen， but also to producing aquatic products with low aller－ genicity.