R. Levy et al., SPECIFICITY OF AN ANTI-ALUMINUM MONOCLONAL-ANTIBODY TOWARD FREE AND PROTEIN-BOUND ALUMINUM, Journal of inorganic biochemistry, 69(3), 1998, pp. 159-163
Anti-aluminium monoclonal antibodies (mAbs) were prepared using alumin
ium chloride-bovine serum albumin complex (Al-BSA) as immunogen. Compe
titive enzyme-linked immunosorbant assay (ELISA), using an Al-BSA coat
ed immunoplate, demonstrated that mice immune sera showed stronger rea
ctivity to AlCl3 than to BSA. Supernatants from hybridomas prepared fr
om cloned anti-Al antibody-producing cells reacted ir. ELISA assays wh
ether the metal was bound to proteins like calmodulin (CaM) and S100b
protein or to immunogen BSA. Moreover, addition of citrate, a potent l
igand for trivalent cations, resulted in a significant withdrawal in m
Ab recognition of aluminium which was previously bound to either CaM o
r S100b proteins. The anti-Al mAbs also reacted with aluminosilicate c
omplexes formed from aluminium chloride and silicic acid. The results
indicate that the monoclonal antibodies recognized aluminium alone, al
uminium bound to silicate, or aluminium bound to a protein core and th
us may be used as an immunologic tool for identifying aluminium in bot
h in vitro and in vivo systems. (C) 1998 Elsevier Science Inc. All rig
hts reserved.