Crosslinking of Cys-Mutated Human Galectin-1 to the Model Glycoprotein Ligands Asialofetuin and Laminin by Using a Photoactivatable Bifunctional Reagent

Mayumi Tamura, Tomoe Watanabe, Takanori Igarashi, Tomoharu Takeuchi, Ken-ichi Kasai, Yoichiro Arata
2014 Biological and Pharmaceutical Bulletin  
Galectins are a group of animal lectins characterized by their specificity for β-galactosides. In our previous study, we showed that a human galectin-1 (hGal-1) mutant, in which a cysteine residue was introduced at Lys 28 , forms a covalently cross-linked complex with the model glycoprotein ligands asialofetuin and laminin by using the photoactivatable sulfhydryl reagent benzophenone-4-maleimide (BPM). In the present study, we used several hGal-1 mutants in which single cysteine residues were
more » ... troduced at different positions and examined their ability to form a covalent complex with asialofetuin or laminin by using BPM. We found that the efficiency of formation of the cross-linked products differed depending on the positions of the cysteine introduced and also on the ligand used for crosslinking. Therefore, by using different cysteine hGal-1 mutants, the chances of isolating different ligands for hGal-1 should increase depending on the systems and cells used.
doi:10.1248/bpb.b13-00876 pmid:24790011 fatcat:2jaazz5e7bdfbb2ck2h3j6dv3y