| Isolation and characterization of Microsporum gypseum lysosomes: role of lysosomes in macroconidia germination. | |
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MedLine Citation:
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PMID: 4336109 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Three types of lysosomes containing either acid protease, alkaline protease, or phosphodiesterase were isolated from a Microsporum gypseum macroconidial homogenate on Ficoll gradients. The acid protease was contained in an assimilative lysosome since its activity was affected by the complexity of the exogenous nitrogen source. Ultracentrifugation and electron microscopy revealed that the alkaline protease-containing vesicles were associated with the spore coat material prior to macroconidial germination. During macroconidial germination, zones of spore coat hydrolysis were seen surrounding these vesicles. Other larger vesicles, believed to contain the phosphodiesterase, were also observed in the spore coat during macroconidial germination. |
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Authors:
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W J Page; J J Stock |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Journal of bacteriology Volume: 110 ISSN: 0021-9193 ISO Abbreviation: J. Bacteriol. Publication Date: 1972 Apr |
Date Detail:
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Created Date: 1972-06-20 Completed Date: 1972-06-20 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2985120R Medline TA: J Bacteriol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 354-62 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acid Phosphatase
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analysis Centrifugation, Density Gradient Hydrogen-Ion Concentration Lysosomes / enzymology, physiology* Microscopy, Electron Microsporum / cytology*, enzymology, growth & development, physiology Models, Biological Peptide Hydrolases / analysis, isolation & purification Phosphoric Diester Hydrolases / analysis, isolation & purification Protein Binding Spores / growth & development* Spores, Fungal / enzymology, growth & development, physiology Ultracentrifugation |
| Chemical | |
Reg. No./Substance:
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EC 3.1.3.2/Acid Phosphatase; EC 3.1.4.-/Phosphoric Diester Hydrolases; EC 3.4.-/Peptide Hydrolases |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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