By Sepharose 4B-thyroglobulin affinity column chromatography a lectin was purified from Bellamya purificata. It showed a single band on alkaline PAGE. This lectin (BPL) agglutinated red blood cells of rabbit,duck and pig,but not of human blood types or formalin and/or glutaraldehyde-fixed rabbit erythrocytes. Its agglutination activity could be inhibited by 1.0mol/L lactose or galactose as well as 60g/L thyroglobulin, but not by alkaline borate buffer.BPL was temperature-sensitive,while showed a broad optical pH range (pH4.56-9.96).
Zhang Jiqiang, Li Qingyi. A Preliminary Study on Bellamy purificata Lectin[J]. Progress in Biochemistry and Biophysics,1995,22(3):281-283
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