Antigen-Binding Specificity of Isolated Cell-Surface Immunoglobulin from Thymus Cells Activated to Histocompatibility Antigens
AUTOR(ES)
Cone, Robert E.
RESUMO
Lactoperoxidase-catalyzed radioiodination of cell-surface proteins was used in the isolation of cell-surface immunoglobulin from thymus-derived thoracic duct lymphocytes activated to histocompatibility-2 antigens. Immunoglobulin was identified by specific precipitation with antiserum to mouse immunoglobulin. Polyacrylamide gel electrophoresis of reduced and alkylated precipitates showed that the immunoglobulin molecules possessed μ-type heavy chains and light chains. Cell-surface immunoglobulin isolated from thymus-derived cells activated to histocompatibility-2 antigens possessed binding specificity for the activating antigens.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=426987Documentos Relacionados
- Cell-Surface Immunoglobulin of Human Thymus Cells and Its Biosynthesis In Vitro
- Single amino acid substitution altering antigen-binding specificity.
- Antigen-binding mutants of mouse myeloma cells.
- Related cell-surface antigens expressed with positional specificity in Drosophila imaginal discs.
- Demonstration That Antigen-Binding Cells Are Precursors of Antibody-Producing Cells After Purification with a Fluorescence-Activated Cell Sorter