Premium
Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down‐regulation
Author(s) -
Ceriani Carolina,
González Nélida S.,
Algranati Israel D.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80253-d
Subject(s) - crithidia fasciculata , ornithine decarboxylase , putrescine , cycloheximide , crithidia , biochemistry , ornithine decarboxylase antizyme , polyamine , biology , adenosylmethionine decarboxylase , enzyme , protein biosynthesis , ornithine , spermine , specific activity , amino acid , protozoa , botany , arginine
Ornithine decarboxylase (ODC) of Crithidia fasciculata extracts shows maximal activity during exponential growth of the parasite and decreases markedly in the stationary phase. The inhibition of protein synthesis by cycloheximide evoked a rapid loss of enzyme activity with a half‐life of about 30 min. Upon removal of DFMO from Crithidia cultures treated with the drug for 24 h, the ODC activity increased at the same rate as total protein synthesis. The addition of putrescine at high concentrations to parasites cultivated in a synthetic medium showed that Crithidia CDC levels were not reduced by polyamines.