An antibody can be specifically oxidized with periodate (NaIO4) on the carb
ohydrate side chains at its C-terminal. Rabbit anti-hepatitis B surface ant
igen (anti-HBsAg) IgG antibodies were bound to the silicon wafer surface by
covalent bonds between aldehydes generated on the carbohydrate side chains
of the antibodies and the reactive amine groups of 3-aminopropyltriethoxyl
silane(APTES)-modified silicon wafer surfaces. A control experiment was als
o performed by direct attachment of antibodies to glutaraldehyde-treated si
licon surfaces. Two different coupling antibody strategies were investigate
d in this paper. Atomic force microscopy was used to observe the orientatio
n of the site-directed and random attachment of rabbit anti-HBsAg IgG antib
odies and the conservation of their antigen-binding capacity (AgBC) was ass
essed using an enzyme immunoassay (EIA).