Separation of two proteins required for synthesis of spermidine from S-adenosyl-L-methionine and putrescine in rat prostate

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Abstract

An enzyme catalyzing transfer of a propylamino group from exogenous decarboxylated S-adenosyl methionine to putrescine to form spermidine (spermidine synthase) has been separated from the putrescine-activated S-adenosyl methionine decarboxylase in soluble extracts of rat ventral prostate. Neither enzyme alone catalyzes the formation of significant quantities of spermidine from S-adenosyl methionine and putrescine, a reaction which proceeds readily on addition of suitable proportions of the two separable enzymes. Aspects of the interaction of these two proteins in the biosynthesis of spermidine by rat prostate are discussed.

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This work was supported in part by a Research Grant (HD-04592) from the U. S. Public Health Service.

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