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Binding studies on a mouse-myeloma immunoglobulin A having specificity for beta-D-(1 yields 6)-linked
The free energies of binding between immunoglobulin A J539 (Fab') and methyl 6-O-acetyl beta-D-galactopyranoside (1) and 6-O-beta-D-galactopyranosyl-1, 2:3, 4-di-O-isopropylidene-alpha-D-galactopyranose (2) have been measured. The values found suggest that bulky substitution on O'-6 or O-1, O-2, O-3, and O-4 in the hapten 6-O-beta-D-galactopyranosyl-D-galactose (3) does not interfere with effective binding of that ligand and the immunoglobulin. This conclusion supports the postulations that (a) the ligand 3 binds only on one side of the molecule, and (b) the combining site of the immunoglobulin J539 appears to be located on an exposed surface area.
The free energies of binding between immunoglobulin A J539 (Fab') and methyl 6-O-acetyl beta-D-galactopyranoside (1) and 6-O-beta-D-galactopyranosyl-1, 2:3, 4-di-O-isopropylidene-alpha-D-galactopyranose (2) have been measured. The values found suggest that bulky substitution on O'-6 or O-1, O-2, O-3, and O-4 in the hapten 6-O-beta-D-galactopyranosyl-D-galactose (3) does not interfere with effective binding of that ligand and the immunoglobulin. This conclusion supports the postulations that (a) the ligand 3 binds only on one side of the molecule, and (b) the combining site of the immunoglobulin J539 appears to be located on an exposed surface area.