Prepare And Characterize Galactose-binding Proteins In Plant Seeds Using Sepharose CL-6B Affinity Chromatography

The isolation and purification of plant lectins and related research about biological properties of plant lectin has been a research hotspot. There are a variety ways of purification, but are no fixed patterns. Based on characteristics of Sepharose CL-6B withβ-galactosidase bond as a ligand, this paper has purified galactose-binding proteins from the seeds of Ginkgo biloba L. (Semen Ginkgo), Momordica charantial and Ricinus communis, using affinity chromatography, and did preliminary analysis of their relationship in evolution. The results showed that the method can obtain much more purified galactose-binding protein from the crude extract by one step, more effective and efficient than traditional methods. Further analysis showed that the galactose-binding protein from Semen Ginkgo contain only B-chain subunit binding with galactose. Furthermore, the galactose-binding protein from Momordica charantial and Ricinus communis are different types of galactose-binding protein evolved from B-chain subunit, thus displayed various biological functions. This study provided an ideal method for the purification of galactose-binding protein. Moreover, the results supplied useful information for the evolution process of galactose-binding proteins.