Stable ornithine decarboxylase in promastigotes of Leishmania mexicana

Studies on the decarboxylation of ornithine in Leishmania mexicana have shown that this activity corresponds to a true ornithine decarboxylase rather than to an oxidative decarboxylation or aminotransferase reaction, both of which also give rise to the release of CO2. The stoichiometric relationship...

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Detalles Bibliográficos
Autores principales: Sanchez, C.P., Gonzalez, N.S., Algranati, I.D.
Formato: JOUR
Materias:
ornithine decarboxylase
leishmania mexicana
nonhuman
priority journal
protein stability
protozoon
Animal
Carboxy-Lyases
Cell-Free System
Kinetics
Leishmania mexicana
Ornithine Decarboxylase
Protein Denaturation
Pyridoxal Phosphate
Substrate Specificity
Support, Non-U.S. Gov't
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0006291X_v161_n2_p754_Sanchez
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario:Studies on the decarboxylation of ornithine in Leishmania mexicana have shown that this activity corresponds to a true ornithine decarboxylase rather than to an oxidative decarboxylation or aminotransferase reaction, both of which also give rise to the release of CO2. The stoichiometric relationship between substrate and products has indicated that extracts of L. mexicana were able to catalyse the formation of an unknown compound besides putrescine and CO2. The addition of cycloheximide to cultures of L. mexicana allowed us to demonstrate that ornithine decarboxylase degradation in vivo was extremely slow in this parasite. This remarkable stability of the enzyme is only comparable to that found in Trypanosoma brucei and contrasts with the high turnover rate of ornithine decarboxylases of different mammalian cells. © 1989.

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