Interaction of hybridoma antibodies with normal and mutant forms of Escherichia coli recA protein.
We have prepared hybridomas which secrete antibodies against E. coli recA protein, by fusing spleen lymphocytes from immunized mice with P3X63-AG8 myeloma cells. This paper describes a preliminary survey of properties of antibody from a hybridoma population designated 156, which inhibits the strand pairing, strand assimilation, repressor cleavage, and DNA-dependent ATPase activities of recA protein. The 156 antibody consists of one or two species which have been tentatively identified as IgG2b. 156 Globulin reacts 4.6-fold more efficiently with denatured recA protein, and it reacts partially with the native tif-1, lexB30, recA44, and recA629 proteins, as well as with peptide fragments which are not common to all four proteins.
D000483:Alleles; D000818:Animals; D000911:Antibodies, Monoclonal; D001426:Bacterial Proteins / Q000235:genetics* / Q000276:immunology; D002460:Cell Line; D003429:Cross Reactions; D000939:Epitopes / Q000032:analysis*; D004926:Escherichia coli / Q000235:genetics*; D014644:Genetic Variation; D006825:Hybridomas / Q000276:immunology; D008214:Lymphocytes / Q000276:immunology; D051379:Mice; D008807:Mice, Inbred BALB C; D009154:Mutation; D010954:Plasmacytoma / Q000276:immunology; D011938:Rec A Recombinases
D000911:Antibodies, Monoclonal; D001426:Bacterial Proteins; D000939:Epitopes; D011938:Rec A Recombinases