Rapid and convenient method for the assay of aminopropyltransferases
- 1 March 1978
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 169 (3) , 709-712
- https://doi.org/10.1042/bj1690709
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. 1,3-Diaminopropane 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.This publication has 16 references indexed in Scilit:
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