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Published January 1978 | public
Journal Article

Magnetic resonance studies of the binding site interactions between ^(19)F-labeled nitrophenyl haptens and specific mouse myeloma immunoglobulin MOPC-315

Abstract

The interactions between MOPC-315, a mouse myeloma protein with specificity for nitrophenyl haptens, and ^(19)F-substituted haptens have been investigated using nuclear magnetic resonance (NMR) spectroscopy. The haptens studied are mono- or dinitrophenyl derivatives of γ-aminobutyric acid, lysine, or glycine which have trifluoromethyl groups attached to the phenyl rings. Upon binding to immunoglobulin, the ^(l9)F nucleus experiences a downfield shift whose magnitude depends on the position of the trifluoromethyl group on the phenyl ring but is independent of other structural changes in the hapten such as the number of nitro groups attached to the phenyl ring. Further, the chemical shift of bound hapten is not influenced by the amount of the constant region attached to the binding site; we accordingly conclude that the presence of the distal, constant regions of the immunoglobulin molecule does not influence binding site interactions.

Additional Information

© 1978 American Chemical Society. Received March 11, 1977. The authors wish to thank Dr. Michael A. Raftery for the use of his fluorescence spectrophotometer and Jack Welch and David Collier for their technical assistance. Contribution No. 5495 from the Church Laboratory of Chemical Biology, Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91 125. Received March 11, 1977. This work was supported by the President's Fund of Caltech and by the National Institutes of Health Grant GM-16424.

Additional details

Created:
August 19, 2023
Modified:
October 23, 2023