Hybrid immunoglobulin isotypes of identical specificity produced by genetic recombination in Escherichia coli and expression in lymphoid cells

We have produced a series of hybrid IgG1‐IgG2a mouse immunoglobulins with identical light chains (L) and variable regions to facilitate the identification of structural features associated with functional differnces between immunoglobulin isotypes. Hybrid heavy chain (H) constant region gene segment...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1987, Vol.2 (2), p.81-89
Hauptverfasser:	Schneider, William P., Oi, Vernon T., Yanofsky, Charles
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Antibody Specificity Binding Sites, Antibody Biological and medical sciences Biotechnology Cloning, Molecular compatible plasmids dansyl Disulfides Escherichia coli Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Genetic engineering Genetic technics hybrid immunologlobulin Immunoglobulin Isotypes - biosynthesis Immunoglobulin Isotypes - genetics Methods. Procedures. Technologies Mice Molecular Sequence Data mouse IgG1 mouse IgG2a Protein Conformation Recombinant Proteins - biosynthesis Recombinant Proteins - genetics Staphylococcal Protein A - immunology Structure-Activity Relationship transfection
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