Structural-Specificity Relationships of the Immunoglobulin Molecule and the Solid Phase Peptde Synthesis of Two Antigen-Binding Peptides
Loading...
Authors
Tippett, Peter S.
Issue Date
1975
Type
Thesis
Language
en_US
Keywords
Alternative Title
Abstract
Recent immunoglobulin structural-functional information
was reviewed with special emphasis on x-ray crystallographic
data from the binding region of the antibody molecule.
Structure-specificity relationships between phosphorylcholine
binding immunoglobulins were discussed and possible
immunoglobulin synthetic approaches including hypervariable
region, active half-molecule, and half-molecule bi-layer
syntheses were proposed. The course of the solid phase
peptide syntheses of peptides including the first and third
hypervariable regions of the heavy chain of M603 were followed
by a modified form of the picrate monitoring procedure of
Gisin and a Schwartz-Mann automated peptide synthesizer
was modified to allow for complete automated cycling of this
picrate monitoring procedure. "Normal" amino acid coupling
characteric curves were defined and the coupling characteristics
of a newly protected amino acid, Trp-For, were documented.
Problems with the coupling of Asn and Arg were discussed
and a mechanism for an unwanted side reaction involving
the methionine side chain was studied. A method for estimating
the number of deletion peptides contaminating the end product
in solid phase peptide synthesis was proposed as was a new
dimerization purification technique involving cysteine
oxidation in peptides.
Description
vii, 121 p.
Citation
Publisher
Kalamazoo College
License
U.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder.