| Comparison of ornithine decarboxylase from rat liver, rat hepatoma and mouse kidney. | |
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MedLine Citation:
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PMID: 3994674 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Comparisons were made of ornithine decarboxylase isolated from Morris hepatoma 7777, thioacetamide-treated rat liver and androgen-stimulated mouse kidney. The enzymes from each source were purified in parallel and their size, isoelectric point, interaction with a monoclonal antibody or a monospecific rabbit antiserum to ornithine decarboxylase, and rates of inactivation in vitro, were studied. Mouse kidney, which is a particularly rich source of ornithine decarboxylase after androgen induction, contained two distinct forms of the enzyme which differed slightly in isoelectric point, but not in Mr. Both forms had a rapid rate of turnover, and virtually all immunoreactive ornithine decarboxylase protein was lost within 4h after protein synthesis was inhibited. Only one form of ornithine decarboxylase was found in thioacetamide-treated rat liver and Morris hepatoma 7777. No differences between the rat liver and hepatoma ornithine decarboxylase protein were found, but the rat ornithine decarboxylase could be separated from the mouse kidney ornithine decarboxylase by two-dimensional gel electrophoresis. The rat protein was slightly smaller and had a slightly more acid isoelectric point. Studies of the inactivation of ornithine decarboxylase in vitro in a microsomal system [Zuretti & Gravela (1983) Biochim. Biophys. Acta 742, 269-277] showed that the enzymes from rat liver and hepatoma 7777 and mouse kidney were inactivated at the same rate. This inactivation was not due to degradation of the enzyme protein, but was probably related to the formation of inactive forms owing to the absence of thiol-reducing agents. Treatment with 1,3-diaminopropane, which is known to cause an increase in the rate of degradation of ornithine decarboxylase in vivo [Seely & Pegg (1983) Biochem. J. 216, 701-717] did not stimulate inactivation by microsomal extracts, indicating that this system does not correspond to the rate-limiting step of enzyme breakdown in vivo. |
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Authors:
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J E Seely; L Persson; G J Sertich; A E Pegg |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Biochemical journal Volume: 226 ISSN: 0264-6021 ISO Abbreviation: Biochem. J. Publication Date: 1985 Mar |
Date Detail:
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Created Date: 1985-05-24 Completed Date: 1985-05-24 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 577-86 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Diamines / pharmacology Electrophoresis, Polyacrylamide Gel Immunoelectrophoresis Kidney / enzymology* Liver / drug effects, enzymology* Liver Neoplasms, Experimental / enzymology* Male Microsomes, Liver / enzymology Ornithine Decarboxylase / immunology, metabolism* Rats Rats, Inbred BUF |
| Grant Support | |
ID/Acronym/Agency:
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1T32 HL-0723/HL/NHLBI NIH HHS; CA18138/CA/NCI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Diamines; 109-76-2/trimethylenediamine; EC 4.1.1.17/Ornithine Decarboxylase |
| Comments/Corrections | |
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