Magnetic resonance studies of the binding site interactions between phosphorylcholine and specific mouse myeloma immunoglobulin
- Creators
- Goetze, A. M.
- Richards, J. H.
Abstract
The interaction of phosphorylcholine-binding mouse myeloma protein M603 and the isotopically substituted hapten phosphoryl[rnethyl-^(13)C]choline has been investigated using ^(13)C and ^(31)P nuclear magnetic resonance (NMR) spectroscopy. Upon binding to antibody, upfield shifts of 0.7 and 1.5 ppm are observed for the hapten ^(13)C and ^(31)P resonances, respectively, and both spectra are in the "slow" exchange limit. Linewidth analysis indicates some immobilization of the phosphate group but essentially unrestricted methyl group rotation for the bound hapten. Hapten-antibody dissociation rate constants of 10 and 38 s^(-1) are calculated from ^(13)C and ^(31)P NMR spectra, respectively, suggesting the possibility of differential dissociation rates for the two opposing ends of the phosphorylcholine molecule. The NMR data are entirely consistent with the known x-ray structure of the M603 Fab'-phosphorylcholine complex (Segal, D. M., Padlan, E. A., Cohen, G. H., Rudikoff, S., Potter, M., and Davies, D.R. (1974), Proc. Natl. Acad. Sci. U.S.A. 71, 4298).
Additional Information
© 1977 American Chemical Society. Received July 22. 1976. Supported by grants from the President's Fund of Caltech and the United States Public Health Service (NIGM-16424 and NIAI 01339).Additional details
- Eprint ID
- 57044
- Resolver ID
- CaltechAUTHORS:20150428-104629036
- Caltech President's Fund
- NIGM-16424
- United States Public Health Service
- NIAI 01339
- United States Public Health Service
- Created
-
2015-04-28Created from EPrint's datestamp field
- Updated
-
2021-11-10Created from EPrint's last_modified field
- Other Numbering System Name
- Caltech Church Laboratory of Chemical Biology
- Other Numbering System Identifier
- 5380