Magnetic Resonance Studies of the Binding Site Interactions Between ¹⁹F Labelled Nitrophenyl Haptens and Specific Mouse Myeloma Immunoglobulin MOPC-315

Author: Kooistra, Dale Alvin

Year: 1978

Degree: Dissertation (Ph.D.)

Advisor: Richards, John H.

Committee Member: Unknown, Unknown

Option: Chemistry

DOI: 10.7907/mrcx-hr46

Abstract

The interactions between MOPC-315, a mouse myelorna protein with specificity for nitrophenyl haptens, and ¹⁹F 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 that have trifluoromethyl groups attached to the phenyl rings. Upon binding to immunoglobulin, the ¹⁹F 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.

Files

• Kooistra_DA_1978.pdf (application/pdf)