PREPARATION AND CHARACTERIZATION OF ANTIPEPTIDE ANTIBODIES DIRECTED AGAINST HUMAN PHENOL AND HYDROXYSTEROID SULFOTRANSFERASES

Sulphotransferases (STs) catalyze the sulphation and, in general, deto xication of a large number of xenobiotics and endogenous compounds. A total of six synthetic peptides derived from the cDNA-derived amino ac id sequences of the human phenol-sulphating form of phenolsulphotransf erase (P-PST) and human hydroxysteroid sulphotransferase (HST)-three f rom each sequence-were separately conjugated to the carrier protein ke yhole limpet hemocyanin, and used to immunize rabbits. One successful antibody preparation was produced from among the P-PST peptides, and t wo from the HST peptides. On immunoblot analysis following SDS/PAGE, t he anti-P-PST antibodies recognized two major forms of phenol ST in ma n, P-PST and the monoamine-sulphating form of PST, M-PST, and the two antibody preparations against HST recognized the human HST. These expe riments demonstrate that it is possible to design specific antibodies against human sulphotransferases based on their amino acid sequences.