Abstract
A soluble beta-galactoside binding 14.5 kDa lectin was purified from the heart of Capra hircus. Its metal independent nature, preferential affinity for beta-d-lactose and 90-94% homology with carbohydrate recognition domain of previously reported galectin-1 confirmed its inclusion in galectin-1 subfamily. The secondary structures of the deduced amino acid sequences were generally conserved with previously reported Gal-1. Exposure of the purified protein to varying temperature and pH, oxidant, thiol blocking reagents, denaturants and detergents resulted in significant changes in UV (ultraviolet), fluorescence, CD (circular dichroism) and FTIR (fourier transform infra red) spectra, thus strongly emphasizing the vitality of regular secondary structure of galectins for maintaining their active conformation. Bioinformatics studies corroborated the results obtained in wet lab. Our findings based on physico-chemical properties, oxidative inactivation and structural analysis of the goat heart galectin-1 suggests significant implications in potential biological and clinical applications.