Isolation of Picomolar Affinity Anti-c-erbB-2 Single-chain Fv by Molecular Evolution of the Complementarity Determining Regions in the Center of the Antibody Binding Site

1996 ◽  
Vol 263 (4) ◽  
pp. 551-567 ◽  
Author(s):  
Robert Schier ◽  
Adrian McCall ◽  
Gregory P. Adams ◽  
Keith W. Marshall ◽  
Hanne Merritt ◽  
...  
Keyword(s):  
Molecular Evolution ◽  
Binding Site ◽  
Antibody Binding ◽  
Single Chain ◽  
Antibody Binding Site ◽  
Single Chain Fv ◽  
Complementarity Determining Regions

Fine tuning of an anti-testosterone antibody binding site by stepwise optimisation of the CDRs

1998 ◽  
Vol 4 (1) ◽  
pp. 59-69 ◽  
Author(s):  
Ari Hemminki ◽  
Seija Niemi ◽  
Lasse Hautoniemi ◽  
Hans Söderlund ◽  
Kristiina Takkinen
Keyword(s):  
Binding Site ◽  
Antibody Binding ◽  
Fine Tuning ◽  
Antibody Binding Site

scholarly journals The antibody binding site. Labelling of a specific antibody against the photo-precursor of an aryl nitrene

1972 ◽  
Vol 128 (3) ◽  
pp. 499-508 ◽  
Author(s):  
G. W. J. Fleet ◽  
J. R. Knowles ◽  
R. R. Porter
Keyword(s):  
Binding Site ◽  
Heavy Chain ◽  
Association Constant ◽  
Hypervariable Region ◽  
Antibody Binding ◽  
Light Chains ◽  
Small Peptides ◽  
Group 4 ◽  
Antibody Binding Site ◽  
Specific Rabbit

The isolation of specific rabbit antibodies for the haptenic group 4-azido-2-nitrophenyl, is described. These antibodies bind 1.8–2.0mol of hapten [∈-(4-azido-2-nitrophenyl)-l-lysine]/mol with an association constant of nearly 107m-1 at 4°C. On photolysis of the antibody–hapten complex, resulting in the formation of an aryl nitrene at the binding site, hapten was covalently bound to the antibody, and the antibody binding site was blocked. The ratio of labelling of heavy- and light-chains was 2.5:1. Two small peptides were isolated from digests of labelled heavy-chain, indicating that some 13% of the label in the antibody was attached to cysteine-92 and to alanine-93. These residues are adjacent to the major hypervariable region in rabbit heavy-chain (residues 95–105).

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