Linked Life Data

2383305

Source:http://linkedlifedata.com/resource/pubmed/id/2383305

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1990-9-13
pubmed:abstractText
Ethyl N-N-benzyl-methyl-oxamate is a N-substituted derivative of the oxamic acid, well-known as inhibitor of the lactate dehydrogenase activity. The biochemical and ultrastructural effects of this drug in Echinococcus multilocularis metacestodes and the repercussions in the livers of receptive host, Meriones unguiculatus, were investigated. This compound decreased the specific activity of the lactate dehydrogenase in the metacestodes and the host liver by 81 and 86.8%, respectively. This N-methyl compound has shown an important repercussion on the lactate dehydrogenase activity due to its greater lipophilicity and thus allows a better penetration of the molecule. In the host liver, a fall of the alkaline and acid phosphatases activity was observed. The glucose and glycogen concentrations were also decreased. The ultrastructural study provided an alteration of the tegument of the metacestodes and damages of the muscular system. The parenchyma was disorganized. In conclusion, these biochemical and ultrastructural data obtained with ethyl-N-N-benzyl-methyl oxamate in E. multilocularis metacestodes show clearly the importance of the lactate dehydrogenase activity in the metacestodes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0004-4172
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
607-10
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Effects of ethyl N-N-benzyl-methyl-oxamate in Meriones unguiculatus infected with Echinococcus multilocularis metacestodes. Biochemical and ultrastructural observations.
pubmed:affiliation
Département de Parasitologie et Pathologie Exotique, Universitaire Rockefeller, Lyon, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't