Dissociation of putrescine-activated decarboxylation of S-adenosyl-L-methionine from the enzymic synthesis of spermidine and spermine by purified prostatic enzyme preparations

Abstract The S-adenosyl-L-methionine decarboxylase that is specifically activated by putrescine or spermidine has been purified more than 500-fold from rat ventral prostate by a new procedure. At later stages of the purification, stoichiometric coupling of S-adenosyl-methionine decarboxylation and the synthesis of spermidine (in the presence of putrescine) and of spermine (in the presence of spermidine) is lost. Certain properties of the purified decarboxylase are described.