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Selective Chemical Catalysis by an Antibody
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 ( k cat ) = 0.4 min-1 and Michaelis constant ( K m ) = 208 μ M , showed substrate specificity, and was inhibited by p -nitrophenylphosphorylcholine. The rate of the reaction was first order in hydroxide ion concentration between p H 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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Cites
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Corbett, P. T., Leclaire, J., Vial, L., West, K. R., Wietor, J.-L., Sanders, J. K. M., & Otto, S. (2006) · Chemical Reviews · doi:10.1021/cr020452p · Cited by 1,922
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Hermann, T., & Patel, D. J. (2000) · Science · doi:10.1126/science.287.5454.820 · Cited by 1,650
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Christianson, D. W. (2006) · Chemical Reviews · doi:10.1021/cr050286w · Cited by 788
At the Crossroads of Chemistry and Immunology: Catalytic Antibodies
Lerner, R. A., Benkovic, S. J., & Schultz, P. G. (1991) · Science · doi:10.1126/science.2024118 · Cited by 668
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Metadata
- Authors
- Pollack, S. J., Jacobs, J. W., & Schultz, P. G.
- Venue
- Science
- Published
- 1986-12-19
- Volume
- 234
- Issue
- 4783
- Pages
- 1570-1573
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1986983782
- Cited by
- 631
- References
- 1
- FWCI
- 21.89
- Type
- journal article
- Language
- en
- Open access
- closed
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- Pollack, S. J., Jacobs, J. W., & Schultz, P. G. (1986). Selective Chemical Catalysis by an Antibody. Science. https://doi.org/10.1126/science.3787262
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