A Waldenström Macroglobulin Which Binds Nitrophenyl Ligands

摘要: Abstract The binding properties of a human Waldenstrom macroglobulin (γMwag), which was fortuitously found to bind nitrophenyl derivatives, have been studied. valences the pentamer γM, cysteine-produced subunit γMs, and tryptic fragments F(ab')2µ Fabµ were 10, 2, 1, respectively. association constant homogeneous equalled 3.8 x 104 m-1 for fragments, subunits, pentamer. Binding manifested by shift in absorption spectrum bound ligand ability latter partially quench fluorescence protein. relative affinity γMwag over 60 ligands studied equilibrium dialysis, inhibition 125I-γMwag precipitation with dinitrophenyl-bovine γ-globulin conjugate, or both. Considerable evidence stereospecific found. By virtue specificity activity, location sites Fab portion molecule, valence one combining site each heavy-light chain pair, this protein has fundamental characteristics associated conventionally induced antibodies.