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Article

Multiple active conformers of mouse ornithine decarboxylase.

The Biochemical journal - 1 Jul 1993

Tsirka S E, Turck C W, Coffino P

Abstract excerpt

Purified recombinant mouse ornithine decarboxylase (ODC) was denatured with urea or with guanidinium chloride. Enzymic activity was efficiently recovered upon dilution of the denaturing agent. ODC renatured after urea treatment was further characterized. Kinetics of decarboxylation of the natural substrate ornithine or of the suicide substrate alpha-difluoromethylornithine (DFMO) were not significantly changed by...

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Identifiers

PMID: 8328969
DOI: 10.1042/bj2930289
PMCID: PMC1134353

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Multiple active conformers of mouse ornithine decarboxylase.PMID 8328969Read ↗

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Structural elements of the ubiquitin-independent proteasome degron of ornithine decarboxylase.Semantic proximity Read ↗

Structure/function relationship studies on the T/S residues 173-177 of rat ODC.Semantic proximity Read ↗

Critical factors governing the difference in antizyme-binding affinities between human ornithine decarboxylase and antizyme inhibitor.Semantic proximity Read ↗

Stable ornithine decarboxylase in a rat hepatoma cell line selected for resistance to alpha-difluoromethylornithine.Semantic proximity Read ↗

Multiple regulation of ornithine decarboxylase in enzyme-overproducing cells.Semantic proximity Read ↗

Formation of functional cross-species heterodimers of ornithine decarboxylase.Semantic proximity Read ↗

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