Document Detail


Tricarboxylic acid cycle enzymes in the plerocercoid of Ligula intestinalis (Cestoda: Pseudophyllidea).
MedLine Citation:
PMID:  1114868     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
All enzymes of the tricarboxylic acid cycle are present in subcellular fractions of the plerocercoid of Ligula intestinalis but the low activity of aconitase and malate dehydrogenase in the forward direction suggests that the complete cycle may be of questionable importance to the parasite. As in other helminths and intertidal molluscs, succinate, formed via a partial reversal of the tricarboxylic acid cycle, is a major end-product of anaerobic glucose degradation.
Authors:
D P McManus
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Zeitschrift für Parasitenkunde (Berlin, Germany)     Volume:  45     ISSN:  0044-3255     ISO Abbreviation:  Z Parasitenkd     Publication Date:  1975  
Date Detail:
Created Date:  1975-05-21     Completed Date:  1975-05-21     Revised Date:  2003-11-14    
Medline Journal Info:
Nlm Unique ID:  8710749     Medline TA:  Z Parasitenkd     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  319-22     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Aconitate Hydratase
Anaerobiosis
Animals
Cell Fractionation
Cestoda / enzymology*
Citric Acid Cycle*
Enzymes / metabolism*
Glucose
Malate Dehydrogenase
Mitochondria / enzymology
Mollusca
Spectrophotometry
Succinates
Chemical
Reg. No./Substance:
0/Enzymes; 0/Succinates; 50-99-7/Glucose; EC 1.1.1.37/Malate Dehydrogenase; EC 4.2.1.3/Aconitate Hydratase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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