Sugawara Kazuharu, Takayanagi Tomoyuki, Kamiya Naoto, Hirabayashi George, Kuramitz Hideki
Faculty of Education, Gunma University, Maebashi, Gunma 371-8510, Japan.
Talanta. 2007 Mar 15;71(4):1637-41. doi: 10.1016/j.talanta.2006.07.046. Epub 2006 Sep 1.
The binding between wheat germ agglutinin (WGA) and N-acetylglucosamine at the electrode covered with chitin film was investigated with voltammetry. Chitin, beta-1,4-poly-N-acetylglucosamine, is one of the biolpolymers which have a high biocompatibility. WGA is immobilized to the surface of chitin film by the affinity of WGA to N-acetylglucosamine residue of chitin. To investigate the binding event of WGA on the chitin modified electrode, N-acetylglucosamine labeled with an electroactive compound was prepared. The binding causes the changes in the electrode response of labeled sugar. The peak current of labeled sugar decreased due to the specific binding with WGA on the chitin film modified at the electrode. N-Acetylglucosamine was successfully determined by using the competitive reaction with labeled sugar to WGA on the chitin film electrode.
