Selective Chemical Catalysis by an Antibody
- 19 December 1986
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 234 (4783) , 1570-1573
- https://doi.org/10.1126/science.3787262
Abstract
The immunoglobulin MOPC167, which binds the transition state analog p-nitrophenylphosphorylcholine with high affinity, catalyzed the hydrolysis of the corresponding carbonate 1. MOPC167 catalysis displayed saturation kinetics with catalytic constant (kcat) = 0.4 min-1 and Michaelis constant (Km) = 208 microM, showed substrate specificity, and was inhibited by p-nitrophenylphosphorylcholine. The rate of the reaction was first order in hydroxide ion concentration between pH 6.0 and 8.0. The lower limit for the rate of acceleration of hydrolysis by the antibody above the uncatalyzed reaction was 770. This study begins to define the rules for the generation of catalytic antibodies.Keywords
This publication has 24 references indexed in Scilit:
- IgG antibodies to phosphorylcholine exhibit more diversity than their IgM counterpartsNature, 1981
- Contributions by ionic and steric features of ligands to their binding with phosphorylcholine-specific immunoglobulin IgA H-8 as determined by fluorescence spectroscopyBiochemistry, 1979
- Molecular studies of subspecificity differences among phosphorylcholine-binding mouse myeloma antibodies using phosphorus-31 nuclear magnetic resonanceBiochemistry, 1978
- Characterization of the "microprotease" from Bacillus cereus. A zinc neutral endoproteaseBiochemistry, 1977
- A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substratesJournal of Molecular Biology, 1977
- Magnetic resonance studies of the binding site interactions between phosphorylcholine and specific mouse myeloma immunoglobulinBiochemistry, 1977
- Fine specificity of rabbit anti-p-azophenylphosphorylcholine antibodies; comparison with HOPC-8 myeloma proteinImmunochemistry, 1976
- Affinity labeling of a phosphorylcholine binding mouse myeloma proteinBiochemistry, 1972
- Specificity for phosphorylchloine of six murine myeloma proteins reactive with Pneumococcus C polysaccharide and β-lipoproteinBiochemistry, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970