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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1989-3-16
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pubmed:abstractText |
The interaction of ricin and its constituent polypeptides, the A- and B-chain, with small unilamellar vesicles of dipalmitoylphosphatidylcholine (DPPC) or dimyristoylphosphatidylcholine (DMPC) was investigated by means of differential scanning calorimetry measurements. The A-chain, at neutral pH, entirely shifted the endothermic peak of small unilamellar vesicles of DPPC from 37 degrees C to 41 degrees C at low protein/lipid ratios. The potency of either ricin or the B-chain to induce the shift of endothermic peak was much less than that of the A-chain. The A-chain was also found to cause mixing of endothermic peaks of DMPC vesicles and DPPC vesicles. These data strongly suggest that the A-chain has the ability to induce fusion of phospholipid vesicles.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
|
pubmed:volume |
242
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
255-8
|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:year |
1989
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pubmed:articleTitle |
Ricin A-chain induces fusion of small unilamellar vesicles at neutral pH.
|
pubmed:affiliation |
Laboratory of Biochemistry, Faculty of Agriculture, Yamaguchi University, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|