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- W1975143587 abstract "This is the first description of the in vitro acetylation of putrescine to monoacetylputrescine. Of the tissues of the rat, homogenates, extracts, and subcellular particles of brain exhibited the highest enzyme activity. In liver homogenates and extracts no acetylputrescine formation was observable, since a degrading process present in the tissue destroyed monoacetylputrescine at a higher rate that it was formed. Liver microsomal preparations, however, were active in catalysing putrescine acetylation, and purified liver cell nuclei were nearly as active as the corresponding brain preparations. These findings together with the low efficacy of arylamines as competitive inhibitors of putrescine acetylation demonstrated that the enzyme responsible for putrescine acetylation is different from the well known acetyl-CoA:arylamine N-acetyltransferase. The physiological role of putrescine acetylation is not yet clear. Both regulatory functions in polyamine metabolism and a role in the physiological inactivation of putrescine is probable." @default.
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- W1975143587 date "1974-07-01" @default.
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- W1975143587 title "Acetyl-CoA:1,4-diaminobutane N-acetyltransferase occurence in vertebrate organs and subcellular localization" @default.
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- W1975143587 doi "https://doi.org/10.1016/0304-4165(74)90007-5" @default.
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