Purification of serine acetyltransferase, a component of a multienzyme complex, by immunoadsorption and selective dissociation of the complex

An immunoadsorbent column chromatography procedure utilizing antibody to one component of a multienzyme complex has been utilized for purification of the second component of this complex. Rabbit immunoglobulin G (IgG) specific for the O-acetylserine sulfhydrylase component of the multienzyme complex cysteine synthetase was linked to Sepharose 4B resin. A crude preparation of cysteine synthetase was bound to a column of IgG-Sepharose, other proteins were removed by washing, and the serine acetyltransferase component of the complex was eluted with 50 m m O-acetylserine, which dissociates the complex of the two enzymes. This purification step produces about a 400-fold increase in specific activity.