Document Detail


Studies on alanine aminotransferase in nematodes.
MedLine Citation:
PMID:  1894437     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
L-alanine aminotransferase was demonstrated in a range of gastrointestinal, free-living and entomophagous nematodes. As in mammals, nematode L-alanine aminotransferase was found to exist in the form of mitochondrial and cytosolic isoenzymes. Whilst the majority of nematode enzymes exhibited a greater overall capacity for L-alanine synthesis than for L-alanine catabolism in vitro, the opposite was true for rat liver L-alanine aminotransferase. In contrast with rat liver, certain gastrointestinal nematodes were apparently able to transaminate D-alanine at low rates. H. contortus cytosolic L-alanine aminotransferase differed significantly from the mammalian enzyme with respect to both thermal stability and response to potential protective reagents.
Authors:
J Walker; J Barrett
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  International journal for parasitology     Volume:  21     ISSN:  0020-7519     ISO Abbreviation:  Int. J. Parasitol.     Publication Date:  1991 Jun 
Date Detail:
Created Date:  1991-10-24     Completed Date:  1991-10-24     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0314024     Medline TA:  Int J Parasitol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  377-80     Citation Subset:  IM    
Affiliation:
Department of Biological Sciences, University College of Wales, U.K.
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MeSH Terms
Descriptor/Qualifier:
Alanine Transaminase / analysis*
Animals
Cytosol / enzymology
Isoenzymes / analysis*
Liver / enzymology
Mitochondria / enzymology
Nematoda / enzymology*
Rats
Chemical
Reg. No./Substance:
0/Isoenzymes; EC 2.6.1.2/Alanine Transaminase

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


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