Abstract: The purification method and bioactivity of shark cartilage angiogenesis inhibitor a(SCAIa) from Guangdong Yangjiang were investigated. The 1.0 mol/Lguanidine and 002 mol/L MES(at 28 ℃ ) extracts of shark cartilage was centrifuged at 6000 r/min for 30 min and the pellet was discarded, and the supernatant was recentrifuged at 12000 r/min for 30 min, then ultrafiltrated and fractionally precipitated with 25%-90% acetone. The precipitate was applied to a Sephadex G 75 gel column and eluted after the predominant peak of A_280nm absorbing material with 0.05 mol/L Tris HCl buffer(containing 0.02mol/L NaCl and 0.02% NaN₃). The material Bwere composed of three single peptides with molecular mass of 18000, 15000 and 12600, then were purified using reverse phase high performance liquid chromatography, the eluate was collected, dried and observed by chichen chorioallantoic membrane. The pure inhibitor was homogeneous as a single band on a silver stained 125% sodium dodecyl sulfate polyacrylamide gel. SCAIa had a molecular weight of 12600. It specifically inhibited the chorioallantoic membrane of chick embryos.

Key words: Shark cartilage, Protein, Purification, Bioactivity