Partial Purification and Characterization of a lectin like protein from Terminalia catappa Seeds

Lectins are proteins having the ability to specifically bind to selective carbohydrates or sugars located on the cell surface and molecules. This binding activity is highly specific, suggesting that each lectin protein is tailored to recognize and interact with a particular type of sugar molecule. The specificity of lectins plays a critical role in various biological processes including cell-to-cell recognition, communication and adhesion. By selectively binding to specific sugars, lectins help to facilitate the exchange of information between cells and molecules, enabling the proper execution of various physiological functions. The research aimed to investigate to partially purify and to characterize lectins from Terminalia catappa seeds. The process involved extracting the lectin from the seeds using physiological saline, partial purification by ammonium sulfate precipitation followed by dialysis. The partially purified lectin extract was tested for multiple parameters. Hemagglutination assay revealed the highest lectin activity for human blood group B+ve, its sugar specificity towards galactose and lactose, loss of its hemagglutination activity by EDTA, enhanced hemagglutination by metal ions like Mg, Cr, Ca, Fe, etc. Effect of pH was found in the range of 4 to 11 and effect of temperature between 20 to 600C. The potential of the lectin for antimicrobial activity against E.coli and S. aureus was assessed by agar well diffusion method. Protein concentration was determined by Lowry's method, performed on a UV-Vis Spectrophotometer (Systronics model number 118).