Monoclonal antibodies to bovine serum albumin: affinity and specificity determinations.
A panel of 12 monoclonal antibodies (MAb) to bovine serum albumin (BSA) was developed and characterized as to their physiochemical and immunological properties. Affinity constants of the MAb varied over a wide range from 10(5) to 10(8) M-1. MAb were assembled into several groups of non- or minimally interacting antibodies by analysis of competitive binding experiments, and BSA domain and subdomain specificities of the MAb were assigned by analysis of results of MAb binding to purified BSA fragments. Further fine specificity delineation was accomplished by examination of cross-reactivity patterns to several mammalian albumins. The data suggest that some of the low affinity MAb recognize sites on different portions of the BSA molecule, indicating that similar epitopes exist on different domains of the BSA molecule.
Morel
G A
GA
Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge 02139.
Yarmush
D M
DM
Colton
C K
CK
Benjamin
D C
DC
Yarmush
M L
ML
D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis / Q000276:immunology*; D000915:Antibody Affinity; D000918:Antibody Specificity; D001667:Binding, Competitive; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004591:Electrophoresis, Polyacrylamide Gel; D007122:Immunoelectrophoresis; D051379:Mice; D008807:Mice, Inbred BALB C; D012710:Serum Albumin, Bovine / Q000276:immunology*; D013045:Species Specificity
D000911:Antibodies, Monoclonal; D012710:Serum Albumin, Bovine