Linked Life Data

8515772

Source:http://linkedlifedata.com/resource/pubmed/id/8515772

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-7-20
pubmed:databankReference
pubmed:abstractText
Similar to the findings obtained with pathogenic Entamoeba histolytica, nonpathogenic isolates were found to kill mammalian cells in vitro, and cell extract caused pore formation in liposome membranes. A pore-forming peptide termed APnp was isolated from a nonpathogenic isolate using the schedule developed for the purification of APp or amoebapore, the homologous peptide of the pathogenic isolate HM-1:IMSS. Compared to APp, the specific activity of APnp in pore formation was 60% lower. cDNA sequencing indicated 95% identity of the primary structures of APnp and APp, and secondary structure predictions revealed a high degree of similarity. Notably, a glutamic acid residue at position 2 of APp is in APnp replaced by proline, which shortens one of the two amphipathic alpha-helices considered crucial for the pore-forming function. This structural divergence of the two peptides might explain the difference in their pore-forming activities.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0166-6851
pubmed:author
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
101-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Comparison of pore-forming peptides from pathogenic and nonpathogenic Entamoeba histolytica.
pubmed:affiliation
Bernhard Nocht Institute for Tropical Medicine, Hamburg, Germany.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro