Partial Purification
and Characterization of a lectin like protein from Terminalia catappa Seeds
Shaikh Fakeha Mohammed Rehan and Uzgare Ashish Sambhaji
Res. J. Chem. Environ.; Vol. 29(7); 117-123;
doi: https://doi.org/10.25303/297rjce1170123; (2025)
Abstract
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).
