| Ultrastructural localization of succinate dehydrogenase in a self-parasitic isolate of Saprolegnia megasperma. | |
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MedLine Citation:
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PMID: 871965 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The enzyme succinate dehydrogenase (SDH, succinate: (acceptor) oxidoreductase, EC 1.3.99.1) was localized by the combined techniques of cytochemistry and electrom microscopy in the hyphae of a self-parasitizing isolate of Saprolegnia megasperma Coker. The enzyme was localized in the mitochondrial membranes; its activity was inhibited by malonate. Electron-dense deposits, whose formation was not prevented by the addition of malonate, appeared outsided of the hyphal cell walls. No evidence was found at the ultrastructural level within the vegetative hyphae for any abnormalities which could be linked to the phenomeonon of self-parasitism. |
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Authors:
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S F Murrin; R A Nolan |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Canadian journal of microbiology Volume: 23 ISSN: 0008-4166 ISO Abbreviation: Can. J. Microbiol. Publication Date: 1977 May |
Date Detail:
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Created Date: 1977-08-25 Completed Date: 1977-08-25 Revised Date: 2000-12-18 |
Medline Journal Info:
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Nlm Unique ID: 0372707 Medline TA: Can J Microbiol Country: CANADA |
Other Details:
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Languages: eng Pagination: 491-6 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Fungi
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enzymology* Mitochondria / enzymology, ultrastructure Oomycetes / enzymology*, ultrastructure Organoids / ultrastructure Succinate Dehydrogenase / isolation & purification* |
| Chemical | |
Reg. No./Substance:
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EC 1.3.99.1/Succinate Dehydrogenase |
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