Photoaffinity labeling studies of the carbohydrate-binding proteins with different affinities.
Photoaffinity labeling has been used as a promising approach to detection and isolation of carbohydrate-binding proteins, which are typically characterized by low binding affinity and selectivity. When there are several specific binding proteins, it is desirable that a photoaffinity probe is capable of simultaneously crosslinking them and that the crosslinking yields depend on the relative binding affinities. In this study, we describe the design and synthesis of carbohydrate photoaffinity probes and their ability to capture lectins of different binding affinities.
Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Naka-cho, 2-24-16, Koganei, Tokyo 184-8588, Japan. Electronic address: sakuraik@cc.tuat.ac.jp.
Kaori
K
Sakurai
Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Naka-cho, 2-24-16, Koganei, Tokyo 184-8588, Japan.
Shimpei
S
Ozawa
Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Naka-cho, 2-24-16, Koganei, Tokyo 184-8588, Japan.
Tamayo
T
Yamaguchi
D010367:Arachis / Q000378:metabolism*; D050260:Carbohydrate Metabolism; D002367:Ricinus communis / Q000378:metabolism; D004895:Erythrina / Q000378:metabolism; D037102:Lectins / Q000378:metabolism*; D008958:Models, Molecular; D019887:Peanut Agglutinin / Q000378:metabolism; D019920:Photoaffinity Labels / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism*; D037121:Plant Lectins / Q000378:metabolism; D011485:Protein Binding
D037102:Lectins; D019887:Peanut Agglutinin; D019920:Photoaffinity Labels; D037121:Plant Lectins; C017707:Ricinus communis agglutinin-1
Carbohydrate-binding proteins; Carbohydrate–protein interaction; Lectin; Photoaffinity labeling; Photoaffinity probes