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.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 5:21 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 13, 2024, 4:14 a.m.) |
Indexed | 1 month, 2 weeks ago (July 14, 2025, 11:34 p.m.) |
Issued | 36 years, 5 months ago (March 17, 1989) |
Published | 36 years, 5 months ago (March 17, 1989) |
Published Print | 36 years, 5 months ago (March 17, 1989) |
@article{Ghoda_1989, title={Prevention of Rapid Intracellular Degradation of ODC by a Carboxyl-Terminal Truncation}, volume={243}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.2928784}, DOI={10.1126/science.2928784}, number={4897}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Ghoda, L. and van Daalen Wetters, T. and Macrae, M. and Ascherman, D. and Coffino, P.}, year={1989}, month=mar, pages={1493–1495} }