Citation
Baldwin-Zuschke, Brenda (1986) Investigations of the effect of antigen binding upon tryptophan reactivity in immunoglobulin G. Master's thesis, California Institute of Technology. doi:10.7907/pwp3-7532. https://resolver.caltech.edu/CaltechTHESIS:04052010-153132274
Abstract
A ^3H/^(14)C-labelled reagent that reacts specifically with tryptophan residues, was used to monitor the reactivity of tryptophans in the Fc and Fab portions of IgG upon binding DNP-gly, (DNP)_1-cytochrome c, and (DNP)_8-cytochrome c. Binding of monovalent antigen caused a decrease in the reactivity of tryptophan residues in the Fc by 18%; binding of multivalent antigen caused decreases in the reactivity of tryptophan residues in Fc by 21% and Fab by 12%. Experiments to elucidate the interaction between IgG and complement component C4 were attempted. Future studies include further characterization of (DNP)_1-cytochrome c and-the complement fixation capability of IgM-ABPC22 with monovalent antigen. Also planned is an investigation of the interaction of C4 with IgM in soluble antibody-antigen complexes.
Item Type: | Thesis (Master's thesis) |
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Subject Keywords: | Chemistry |
Degree Grantor: | California Institute of Technology |
Division: | Chemistry and Chemical Engineering |
Major Option: | Chemistry |
Thesis Availability: | Public (worldwide access) |
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Thesis Committee: |
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Defense Date: | June 1985 |
Record Number: | CaltechTHESIS:04052010-153132274 |
Persistent URL: | https://resolver.caltech.edu/CaltechTHESIS:04052010-153132274 |
DOI: | 10.7907/pwp3-7532 |
Default Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. |
ID Code: | 5691 |
Collection: | CaltechTHESIS |
Deposited By: | Tony Diaz |
Deposited On: | 19 Apr 2010 17:20 |
Last Modified: | 16 Apr 2021 22:14 |
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