Crosslinking of Cys-Mutated Human Galectin-1 to the Model Glycoprotein Ligands Asialofetuin and Laminin by Using a Photoactivatable Bifunctional Reagent
| Autor: | Mayumi Tamura, Yoichiro Arata, Tomoharu Takeuchi, Takanori Igarashi, Ken-ichi Kasai, Tomoe Watanabe |
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| Rok vydání: | 2014 |
| Předmět: |
Galectin 1
Mutant Asialoglycoproteins Pharmaceutical Science Photoaffinity Labels ligand Ligands Maleimides Benzophenones chemistry.chemical_compound Sulfhydryl reagent Humans crosslink Cysteine Fetuins Maleimide Galectin Pharmacology chemistry.chemical_classification galectin Chemistry Ligand General Medicine maleimide Recombinant Proteins Cross-Linking Reagents Biochemistry Covalent bond Mutagenesis Site-Directed Laminin Glycoprotein benzophenone |
| Zdroj: | Biological and Pharmaceutical Bulletin. 37:877-882 |
| ISSN: | 1347-5215 0918-6158 |
| DOI: | 10.1248/bpb.b13-00876 |
| Popis: | 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 introduced 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. |
| Databáze: | OpenAIRE |
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