INVESTIGADORES
RUIZ oscar Adolfo
artículos
Título:
1. Effect of N-alkyl and C-alkylputrescines on the activity of ornithine decarboxylase from rat liver and E.coli.
Autor/es:
OSCAR. A. RUIZ, DANIEL ALONSO-GARRIDO, GRACIELA BULDAIN AND ROSALÍA B. FRYDMAN.
Revista:
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
Referencias:
Año: 1986 vol. 873 p. 53 - 61
ISSN:
0167-4838
Resumen:
N-Methyl, N-ethyl-, N-propyl-, N-butyl, N,N-dimethyl- and N,NŒ-dimethylputrescines were assayed as inhibitors of ornithine decarboxylase (EC 4.1.1.17) from rat liver and from Escherichia coli. They were found to be poor inhibitors, with the exception of N-propylputrescine and N,N-dimethylputrescine, which were inhibitory at 25 mM. A homologous series of 1-alkylputrescines ranging from 1-methylputrescine (1,4-diaminopentane) to 1-heptylputrescine (1,4-diaminoundecane) was assayed for effect on the activity of ornithine decarboxylase from the same sources. 1-methylputrescine (5 mM) inhibited the mammalian enzyme, while the higher homologues showed significantly less inhibitory activity. When assayed on the bacterial enzyme, 1-methylputrescine (5 mM) was not inhibitory, while the higher homologues showed inhibitory effects. At higher concentrations, 1-methylputrescine and 1-heptylputrescine, 2-methylputrescine, inhibitors of these series of rat liver ornithine decarboxylase. When 1-methylputrescine, 2-methylputrescine, 1,2-dimethylputrescine, 1,3-dimethylputrescine and 1,4-dimethylputrescine were assayed as inhibitors of the decarboxylase, 2-methylputrescine was found to be the best inhibitor of the rat liver enzyme, while 1,3-dimethylputrescine was the best inhibitor of the bacterial enzyme. 1,4-Dimethylputrescine (2,5-diaminohexane) did not inhibit the enzyme from either source. Both, 2-methylputrescine and 1-methylputrescine, as well as the 1,2- and 1,3-dimethylputrescines were competitive inhibitors of the enzyme, and a Ki of 1 mM was obtained for 2-methylputrescine when the rat liver  ecarboxylase was used. N-Methyl, 1-methyl and 2-methylputrescines were found to inhibit in vivo the activity of rat liver ornithine decabroxylase which had been previously induced by thioacetamide treatment. 2-Methylputrescine (50 ƒÊmol/100 g body weight) was found to be the best in vivo inhibitor (93% inhibition), while putrescine under similar conditions inhibited 56% of the enzymatic activity.