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Science 19 December 1986:
Vol. 234. no. 4783, pp. 1570 - 1573
DOI: 10.1126/science.3787262

Articles

Science, Vol 234, Issue 4783, 1570-1573
Copyright © 1986 by American Association for the Advancement of Science


articles

Selective chemical catalysis by an antibody

SJ Pollack, JW Jacobs, and PG Schultz

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.


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