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Article

Single amino-acid replacement is responsible for the stabilization of ornithine decarboxylase in HMOA cells.

European journal of biochemistry - 15 Jun 1993

Miyazaki Y, Matsufuji S, Murakami Y, Hayashi S

Abstract excerpt

The half-life of ornithine decarboxylase (ODC) in HMOA cells, a variant cell line derived from hepatoma tissue culture (HTC) cells, is markedly increased compared with that in the parental cell line. In the present study, we examined which of the three relevant factors is responsible for the ODC stabilization in HMOA cells, namely ODC itself, a regulatory protein antizyme and an ODC-degrading activity. SDS/PAGE...

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PMID: 8319692
DOI: 10.1111/j.1432-1033.1993.tb17987.x

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Single amino-acid replacement is responsible for the stabilization of ornithine decarboxylase in HMOA cells.PMID 8319692Read ↗

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

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Characterization of sequences involved in mediating degradation of ornithine decarboxylase in cells and in reticulocyte lysate.Semantic proximity Read ↗

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

Cloning and functional analysis of the rat ornithine decarboxylase-encoding gene.Semantic proximity Read ↗

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

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

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