Abstract
In contrast to the catalytic (alpha) subunit of the Na+/K(+)-ATPase holoenzyme, the glycoprotein (beta) subunit has proven to be a poor antigen for monoclonal antibody (Mab) production. However, in this work six Mabs directed against the beta-subunit of the lamb kidney holoenzyme have been isolated. These Mabs all recognize the holoenzyme, but their 'in solution' binding affinities for deglycosylated enzyme or isolated beta are generally at least 10-fold higher. Species specificity mapping, antibody patterns of binding to beta-fragments and competition binding studies indicated that there were only three distinct epitopes, with two antibodies binding in the NH2-terminal half (epitopes I and II) and 4 Mabs binding at the same or overlapping site (III) in the -COOH terminal half of beta. DNA sequence analysis of isolated collections of bacteriophage M13 that contain a 15 amino-acid 'epitope library' insert in the pIII protein, which enables them to bind to the antibodies, revealed the residues KYRDS (amino acids 111-115) and LETYP (amino acids 197-201) to be the deduced sequences for the epitopes of Mabs M19-P7-E5 (II) and M17-P5-F11 (III), respectively. The epitope I site was not, however, identified. Further studies showed that...Continue Reading
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