Abstract: The isolation, purification, primary structure and anti-oxidation of protein from Pinus koraiensis Sieb.et Zucc. seeds were studied and its function mechanism was discussed. The preliminary classification of the protein was conducted by salting out with ammonium sulfate in the filtrate, then the resulting protein(P₈₀) with the highest collection rate was purified by G-75 gel chromatograph and DEAE-cellulose chromatography,and sample D was separated from P₈₀. Sample D was analyzed by MADIL-TOF-MS. The result showed that sample D and north American white pine nuts Albumin 4 were matched with high scores, and the matched score was 99. And it had the molecular weight of 18 647 u, isoelectric point of 5.35, and the coverage of gene sequence 41%.Based on the matched score and research results, Albumin 4 and sample D were similar and both a kind of pine cone proteins, entitled HSR-Protein 1. In vitro antioxidant experiment showed that Pinus koraiensis Sieb.et Zucc.seeds protein had good scavenging activities of ·OH and O₂^-·. At the concentration of 800 mg/L, the ·OH cleaning rate of pine nut protein component D, protein components P₈₀, and crude protein were 93.12%, 90.89% and 89.12%, respectively. Pine nut protein components D had the strongest scavenging ability of ·OH. At the same concentration, the O₂^-· scavenging rates of pine nut protein component D, component P₈₀, and crude protein were 64.19%, 56.45% and 35.19%, respectively. Pine nut protein components D was the strongest. With the same concentration, the scavenging ability became stronger with the purity increasing.

Key words: protein from Pinus koraiensis Sieb.et Zucc.seeds, isolation, purification, structure analysis, anti-oxidation