Rapid and convenient method for the assay of aminopropyltransferases

H. Hibasami, A. E. Pegg

Research output: Contribution to journalArticlepeer-review

33 Scopus citations


A new method for the assay of aminopropyltransferase activity is described. The method measures the formation of [methyl-14C] methylthioadenosine from decarboxylated S-adenosyl[methyl-14C]methionine in the presence of an amine acceptor. When used with extracts from rat ventral prostate, kidney, liver or brain, and with putrescine or spermidine as amines, the method gave results in excellent agreement with those obtained by the much more time-consuming conventional method. It was found that 1,3-diamino-propane and 1,8-diamino-octane were not acceptors for the prostatic enzyme fraction, but 1,5-diaminopentane (cadaverine) was active and 1,9-diaminononane and 1,12-diaminododecane also lead to the production of [methyl-14C] methylthioadenosine.

Original languageEnglish (US)
Pages (from-to)709-712
Number of pages4
JournalBiochemical Journal
Issue number3
StatePublished - 1978

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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