Abstract
Summary Putrescine-activated S-adenosylmethionine decarboxylase and spermidine and spermine synthases, the enzymes catalyzing the synthesis of spermidine and spermine from S-adenosylmethionine and the appropriate amine, have been separated and partially purified from the soluble fraction of rat liver. During the purification of S-adenosylmethionine decarboxylase the stoichiometry between the decarboxylation of S-adenosylmethionine and the formation of spermidine in the presence of putrescine was lost.
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