rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
1990-6-27
|
pubmed:abstractText |
A primary effect of a novel H-toxin of Clostridium septicum on the hemolysis of rabbit erythrocytes was shown to be the activation of phospholipase A2 (PLA2) associated with rabbit erythrocyte membranes by 20-fold that of controls. Furthermore, the activation of PLA2 induced by the H-toxin was enhanced in the presence of NAD. The H-toxin itself had no PLA2 activity. On the contrary, the H-toxin bound to palmitic acid at a molar proportion of 1:1 and lost its hemolytic activity. The PLA2 was not activated by the H-toxin bound to palmitic acid. These results suggest that activation of the PLA2 is responsible for development of the hemolytic activity of the H-toxin.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0378-1097
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
56
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
319-22
|
pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2341026-Animals,
pubmed-meshheading:2341026-Bacterial Toxins,
pubmed-meshheading:2341026-Clostridium,
pubmed-meshheading:2341026-Enzyme Activation,
pubmed-meshheading:2341026-Erythrocyte Membrane,
pubmed-meshheading:2341026-Hemolysis,
pubmed-meshheading:2341026-NAD,
pubmed-meshheading:2341026-Palmitic Acids,
pubmed-meshheading:2341026-Phospholipases,
pubmed-meshheading:2341026-Phospholipases A,
pubmed-meshheading:2341026-Phospholipases A2,
pubmed-meshheading:2341026-Rabbits
|
pubmed:year |
1990
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pubmed:articleTitle |
Activation of phospholipase A2 in rabbit erythrocyte membranes by a novel hemolytic toxin (H-toxin) of Clostridium septicum.
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pubmed:affiliation |
Department of the Second Microbiology, Chiba University School of Medicine, Japan.
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pubmed:publicationType |
Journal Article
|