Rapid and convenient method for the assay of aminopropyltransferases

H. Hibasami, A. E. Pegg

    Research output: Contribution to journalArticlepeer-review

    33 Scopus citations

    Abstract

    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
    Volume169
    Issue number3
    DOIs
    StatePublished - 1978

    All Science Journal Classification (ASJC) codes

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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