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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1995-4-10
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pubmed:abstractText |
Vibrio parahaemolyticus, an important enteric pathogen, produces toxin (Kanagawa haemolysin, KH), the presence of which correlates well with pathogenicity. KH induced lysis of human red blood cells (HRBC); the kinetics were strongly dependent on KH concentration (0-1 HU/ml) and rather independent of target cell concentration [0.5 < or = haematocrit (%) < or = 6] and the ratio KH:HRBC. The suggestion that KH-induced haemolysis is due to colloid osmosis is supported by results indicating: (1) osmotic protection (by suspension in iso-osmotic choline chloride, D-sorbitol or L-valine, or MOPS-buffered saline with added sucrose), (2) a cell volume increase prior to lysis, and (3) an increase in HRBC cation (86Rb+) influx after KH addition, indicating raised passive cation permeation. The effect of temperature on KH-induced haemolysis indicates the importance of processes other than the action of a simple water-filled pore, because of the high activation energy [53.30 +/- 2.79 kJ (mol.)-1] involved. Although haemolytic rate was attenuated by washout after 5 min KH exposure, the KH-induced lesion itself was not susceptible to washout by either extracellular volume expansion (at constant osmolarity) or centrifugation/resuspension. This suggests that HRBC binding of KH from aqueous solution still continues after 5 min exposure at 37 degrees C. Pre-vortexing KH with dibutyl phthalate (DBP) dramatically reduced the haemolytic activity of the aqueous toxin preparation, suggesting a protein-lipid interaction, which may support the contention that KH can move from a hydrophilic to a hydrophobic environment. Two features were identified that are characteristic of highly purified TDH preparations: (1) thermostability of haemolysin, and (2) monovalent cation selectivity series of lesion: Cs+ > Li+ > K+ > Rb+ > Na+, confirming that TDH is the important leak-inducing agent of KH.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Monovalent,
http://linkedlifedata.com/resource/pubmed/chemical/Choline,
http://linkedlifedata.com/resource/pubmed/chemical/Hemolysin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Rubidium,
http://linkedlifedata.com/resource/pubmed/chemical/Sorbitol,
http://linkedlifedata.com/resource/pubmed/chemical/Valine
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0041-0101
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1397-412
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:7886698-Adult,
pubmed-meshheading:7886698-Cations, Monovalent,
pubmed-meshheading:7886698-Cell Size,
pubmed-meshheading:7886698-Choline,
pubmed-meshheading:7886698-Erythrocytes,
pubmed-meshheading:7886698-Hematocrit,
pubmed-meshheading:7886698-Hemolysin Proteins,
pubmed-meshheading:7886698-Hemolysis,
pubmed-meshheading:7886698-Humans,
pubmed-meshheading:7886698-Isotope Labeling,
pubmed-meshheading:7886698-Kinetics,
pubmed-meshheading:7886698-Osmosis,
pubmed-meshheading:7886698-Rubidium,
pubmed-meshheading:7886698-Sorbitol,
pubmed-meshheading:7886698-Temperature,
pubmed-meshheading:7886698-Valine,
pubmed-meshheading:7886698-Vibrio parahaemolyticus
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pubmed:year |
1994
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pubmed:articleTitle |
Aspects of the haemolytic reaction induced by Kanagawa haemolysin of Vibrio parahaemolyticus.
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pubmed:affiliation |
University Laboratory of Physiology, University of Oxford, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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