Abstract
A V region mutant producing an antibody that had lost the ability to bind phosphocholine was isolated from a hybridoma producing a germline encoded T15 antibody. The mutation resulted in a single aspartic acid to asparagine substitution at residue 95 of the H chain V region. This confirms that the aspartic acid at residue 95 plays a major role in Ag binding. The results also suggest that somatic cell genetic techniques can be used to generate mAb with useful changes in Ag binding.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acids / physiology
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Animals
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Antibodies, Monoclonal / genetics*
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Base Sequence
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Immunoglobulin Variable Region / chemistry
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Immunoglobulin Variable Region / genetics*
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Mice
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Mice, Inbred BALB C
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Molecular Sequence Data
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Mutation
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Phosphorylcholine / immunology*
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Protein Conformation
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Structure-Activity Relationship
Substances
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Amino Acids
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Antibodies, Monoclonal
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Immunoglobulin Variable Region
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Phosphorylcholine
Associated data
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GENBANK/D10148
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GENBANK/D10149
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GENBANK/M58659
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GENBANK/M58674
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GENBANK/M58675
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GENBANK/M60429
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GENBANK/M60430
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GENBANK/M60432
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GENBANK/M60434
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GENBANK/M60435