title: Prevention of rapid intracellular degradation of ODC by a carboxyl-terminal truncation.
abstract: Ornithine decarboxylase (ODC) was converted from a protein with a short intracellular half-life in mammalian cells to a stable protein by truncating 37 residues at its carboxyl terminus. Cells expressing wild-type protein lost ODC activity with a half-life of approximately 1 hour. Cells expressing the truncated protein, however, retained full activity for at least 4 hours. Pulse-chase experiments in which immunoprecipitation and gel electrophoresis were used confirmed the stabilizing effect of the truncation. Thus, a carboxyl-terminal domain is responsible for the rapid intracellular degradation of murine ODC.
authors.affiliation: Department of Microbiology and Immunology, University of California, San Francisco 94143.
authors.forename: L
authors.initials: L
authors.lastname: Ghoda
authors.forename: T
authors.initials: T
authors.lastname: van Daalen Wetters
authors.forename: M
authors.initials: M
authors.lastname: Macrae
authors.forename: D
authors.initials: D
authors.lastname: Ascherman
authors.forename: P
authors.initials: P
authors.lastname: Coffino
mesh_terms: D000818:Animals; D002460:Cell Line; D003001:Cloning, Molecular; D051379:Mice; D009955:Ornithine Decarboxylase / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D013329:Structure-Activity Relationship; D014162:Transfection
chemical_list: D011994:Recombinant Proteins; D009955:Ornithine Decarboxylase