Cross-Link Formation between Mutant Galectins of Caenorhabditis elegans with a Substituted Cysteine Residue and Asialofetuin via a Photoactivatable Bifunctional Reagent

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概要

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• LEC-1 is the first tandem repeat-type galectin isolated from an animal system; this galectin has two carbohydrate recognition domains in a single polypeptide chain. Because its two lectin domains have different sugar-binding profiles, these domains are thought to interact with different carbohydrate ligands. In our previous study, we showed that a mutant of LEC-1 in which a cysteine residue was introduced at a unique position in the N-terminal lectin domain (Nh) can be cross-linked with a model glycoprotein ligand, bovine asialofetuin, by using a bifunctional photoactivatable cross-linking reagent, benzophenone-4-maleimide. In the present work, we applied the same procedure to the C-terminal lectin domain (Ch) of LEC-1. Cross-linked products were formed in the cases of two mutants in which a cysteine residue was introduced at Lys177 and Ser268, respectively. This method is very useful for capturing and assigning endogenous ligand glycoconjugates with relatively low affinities to each carbohydrate recognition domain of the whole tandem repeat-type galectin molecule.

著者

• Tamura Mayumi

  Department Of Biological Chemistry Faculty Of Pharmaceutical Sciences Teikyo University

• TAMURA Mayumi

  Faculty of Pharmaceutical Sciences, Kanazawa University

• Nonaka Takamasa

  School Of Pharmacy Iwate Medical University

• Kasai Ken-ichi

  Department Of Biological Chemistry Faculty Of Pharmaceutical Sciences Teikyo University

• Arata Yoichiro

  Faculty of Pharmaceutical Sciences, Josai University

• Takeuchi Tomoharu

  Faculty of Pharmaceutical Sciences, Josai University

• Nonaka Takamasa

  School of Pharmacy, Iwate Medical University

• Tamura Mayumi

  Faculty of Pharmaceutical Sciences, Josai University

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