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PMID: 2928784 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Prevention of rapid intracellular degradation of ODC by a carboxyl-terminal truncation.

Science (New York, N.Y.) ·Vol. 243 ·No. 4897 ·1989-03-17 ·Pages 1493-5

Ghoda L, van Daalen Wetters T, Macrae M, Ascherman D, Coffino P

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.

MeSH Terms
Animals Cell Line Cloning, Molecular Mice Ornithine Decarboxylase/genetics,metabolism Recombinant Proteins/metabolism Structure-Activity Relationship Transfection
Chemicals
Recombinant Proteins Ornithine Decarboxylase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Ghoda L
Department of Microbiology and Immunology, University of California, San Francisco 94143.
van Daalen Wetters T
Macrae M
Ascherman D
Coffino P
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1989-03-17
Pages
1493-5
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NCI NIH HHS · CA 09043 · United States
NCI NIH HHS · CA 29048 · United States
NCI NIH HHS · CA 47721 · United States
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