Purification of recA-based fusion proteins by immunoadsorbent chromatography. Characterization of a major antigenic determinant of Escherichia coli recA protein.
Monoclonal antibodies to Escherichia coli recA protein were prepared, characterized, and used as affinity reagents for the purification of recA and recA:somatostatin fusion proteins. The monoclonal antibodies recognize an antigenic determinant or determinants located between amino acids 260 and 330 of recA. Addition of a fragment of the recA gene coding for these amino acids to an unrelated gene (beta-galactosidase) allowed the resulting beta-galactosidase fusion protein to be recognized by the recA monoclonal antibodies.
Krivi
G G
GG
Bittner
M L
ML
Rowold
E
E
Wong
E Y
EY
Glenn
K C
KC
Rose
K S
KS
Tiemeier
D C
DC
D000818:Animals; D000911:Antibodies, Monoclonal; D002846:Chromatography, Affinity / Q000379:methods; D002872:Chromosome Deletion; D000939:Epitopes / Q000032:analysis*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006825:Hybridomas / Q000276:immunology; D051379:Mice; D011938:Rec A Recombinases / Q000276:immunology / Q000302:isolation & purification*; D001616:beta-Galactosidase / Q000235:genetics
D000911:Antibodies, Monoclonal; D000939:Epitopes; D011938:Rec A Recombinases; D001616:beta-Galactosidase