| The noninvolvement of MDH as NAD-oxidoreductase shuttle in rat liver peroxisomes. | |
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MedLine Citation:
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PMID: 6477606 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Subcellular localization of malate dehydrogenase and glycerol-3-phosphate dehydrogenase in rat liver was studied by sucrose density gradient centrifugation. The specific adsorption of cytosolic malate dehydrogenase to the peroxisomes was observed. This phenomenon was eliminated by washing peroxisome-rich fraction with 100 mM potassium chloride. It is suggested that the malate shuttle between the cytosol and the mitochondria is more dominant than the glycerophosphate shuttle with respect to the transfer of reducing equivalents, while NADH produced by fatty acid oxidation in peroxisomes can not be transferred into the cytosol via the malate shuttle in the rat liver. |
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Authors:
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S Horie; H Ishii; S Itoh; T Suga |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Biochemistry international Volume: 8 ISSN: 0158-5231 ISO Abbreviation: Biochem. Int. Publication Date: 1984 Mar |
Date Detail:
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Created Date: 1984-10-19 Completed Date: 1984-10-19 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 8100311 Medline TA: Biochem Int Country: AUSTRALIA |
Other Details:
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Languages: eng Pagination: 353-9 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 Cytosol / enzymology Glycerolphosphate Dehydrogenase / metabolism* Liver / enzymology* Malate Dehydrogenase / metabolism* Male Microbodies / enzymology* NAD / metabolism* Oxidation-Reduction Oxidoreductases / metabolism* Potassium Chloride / pharmacology Rats Rats, Inbred Strains Subcellular Fractions / enzymology |
| Chemical | |
Reg. No./Substance:
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53-84-9/NAD; 7447-40-7/Potassium Chloride; EC 1.-/Oxidoreductases; EC 1.1.-/Glycerolphosphate Dehydrogenase; EC 1.1.1.37/Malate Dehydrogenase |
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