Document Detail


Isolation and characterization of Microsporum gypseum lysosomes: role of lysosomes in macroconidia germination.
MedLine Citation:
PMID:  4336109     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
W J Page; J J Stock
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of bacteriology     Volume:  110     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  1972 Apr 
Date Detail:
Created Date:  1972-06-20     Completed Date:  1972-06-20     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  354-62     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acid Phosphatase / 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:
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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