A surface plasmon resonance assay for the binding of Amaranthus hypochondriacus var. Mexico lectin to glycoprotein.
We have used the analytical system based on surface plasmon resonance to monitor the interaction between Amaranthus hypochondriacus var. Mexico lectin and four different fetuins; fetuin, asialofetuin, agalactofetuin, and agalactosaminofetuin. Agalactofetuin and agalactosaminofetuin were prepared by enzymic digestion of asialofetuin using jack bean beta-galactosidase or endo-alpha-N-acetylgalactosaminidase from Diplococcus pneumoniae. Ligands were immobilized onto a sensor surface via amide linkages. The lectin interacted most strongly with asialofetuin, but not with agalactosaminofetuin. The binding of the lectin to asialofetuin was inhibited by N-acetylgalactosamine or Gal beta 1-->3GalNAc in a dose-dependent manner.
Ozeki
M
M
Department of Agricultural Chemistry, Faculty of Bioresources, Mie University, Japan.
Furuichi
Y
Y
Umekawa
H
H
Takahashi
T
T
D001212:Asialoglycoproteins / Q000378:metabolism; D001667:Binding, Competitive / Q000187:drug effects; D015374:Biosensing Techniques; D060748:Fetuins; D006023:Glycoproteins / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D000509:alpha-Fetoproteins / Q000378:metabolism*
D001212:Asialoglycoproteins; D060748:Fetuins; D006023:Glycoproteins; D037102:Lectins; D010940:Plant Proteins; D000509:alpha-Fetoproteins; C017029:asialofetuin