Production and characterization of monoclonal antibodies to the N-terminal domain of lambda repressor.
Monoclonal antibodies reactive with distinct regions of the N-terminal domain of the lambda repressor protein have been isolated. By comparing the affinities of these antibodies for mutant repressors with increased and decreased thermal stabilities, each of the antibodies can be shown to bind to epitopes accessible in the native conformation of the N-terminal domain. Experiments probing antibody binding to protein fragments, mutant variants, and peptides have also been used to define likely regions of contact between the antibodies and the N-terminal domain.
Breyer
R M
RM
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Sauer
R T
RT
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000032:analysis / Q000096:biosynthesis*; D000914:Antibodies, Viral / Q000032:analysis / Q000096:biosynthesis; D010582:Bacteriophage lambda / Q000276:immunology*; D001666:Binding Sites, Antibody; D001667:Binding, Competitive; D004268:DNA-Binding Proteins; D005260:Female; D051379:Mice; D008807:Mice, Inbred BALB C; D011487:Protein Conformation; D012097:Repressor Proteins / Q000276:immunology* / Q000378:metabolism; D014157:Transcription Factors / Q000276:immunology*; D014764:Viral Proteins / Q000276:immunology* / Q000378:metabolism; D054334:Viral Regulatory and Accessory Proteins
D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral; D004268:DNA-Binding Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins