PLANT BIOCHEMISTRY OF XENOBIOTICS - ISOLATION AND PROPERTIES OF SOYBEAN O-GLUCOSYL AND N-GLUCOSYL AND O-MALONYLTRANSFERASES AND N-MALONYLTRANSFERASES FOR CHLORINATED PHENOLS AND ANILINES

O-Glucosyltransferase (O-GT), O-malonyltransferase (O-MAT), N-glucosyltransferase (N-GT), and N-malonyltransferase (N-MAT) activities have been detected in cultured soybean cells, using pentachlorophenol and 3,4-dichloroaniline as xenobiotic standard substrates. The O-GT was purified ∼ 1000-fold, and the N-MAT ∼ 70-fold. There was an extensive copurification of O-GT and O-MAT. The following functional molecular weight values were obtained, 47 kDA (O-GT), 48 kDA (O-MAT) 43 kDa (N-GT), and 48 kDa (N-MAT). O-GT and N-MAT appeared to be monomeric polypeptides with isoelectric points of ∼4.8 and ∼6.1, respectively. The O-GT, N-GT, and N-MAT activities had marked substrate specificities for chlorinated aromatic xenobiotics and thus illustrate the existence of plant isoenzymes with specificity for xenobiotics. © 1991.