Quantitative estimation of interaction between carbohydrates and concanavalin A by surface plasmon resonance biosensor.
We measured the affinity of more than 20 sugars with concanavalin A (ConA) by an optical biosensor (surface plasmon resonance sensor) using asialofetuin (ASF) as an immobilized binding partner of ConA. We determined kinetic parameters of the effects of sugars on the dissociation of ConA from ASF quantitatively, and the structural requirements of the functional groups of sugars for binding with ConA. We found that the affinity of ConA for sugars is dependent on its conformation induced by interaction with the binding partner. In addition, the results showed that optical biosensor system is well mimics the interaction of ConA with sugars in biomembrane.
Goto
Satoru
S
Faculty of Pharmaceutical Sciences, University of Tokushima, Japan. sgoto@ph.tokushima-u.ac.jp
Masuda
Kyoko
K
Miura
Miyuki
M
Kanazawa
Keiko
K
Sasaki
Miki
M
Masui
Miyuki
M
Shiramizu
Maki
M
Terada
Hiroshi
H
Chuman
Hiroshi
H
D000818:Animals; D001212:Asialoglycoproteins / Q000737:chemistry*; D050260:Carbohydrate Metabolism; D002241:Carbohydrates / Q000737:chemistry*; D002417:Cattle; D003208:Concanavalin A / Q000737:chemistry* / Q000378:metabolism; D004903:Erythrocyte Aggregation; D060748:Fetuins; D006801:Humans; D007700:Kinetics; D011485:Protein Binding; D013329:Structure-Activity Relationship; D020349:Surface Plasmon Resonance; D000509:alpha-Fetoproteins / Q000737:chemistry*
D001212:Asialoglycoproteins; D002241:Carbohydrates; D060748:Fetuins; D000509:alpha-Fetoproteins; C017029:asialofetuin; D003208:Concanavalin A