Purification of recA-based fusion proteins by immunoadsorbent chromatography. Characterization of a major antigenic determinant of Escherichia coli recA protein.

Autor: Krivi, G G, Bittner, M L, Rowold, E, Wong, E Y, Glenn, K C, Rose, K S, Tiemeier, D C
Zdroj: Journal of Biological Chemistry; August 1985, Vol. 260 Issue: 18 p10263-10267, 5p
Abstrakt: 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.
Databáze: Supplemental Index