Linked Life Data

1782805

Source:http://linkedlifedata.com/resource/pubmed/id/1782805

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1992-3-16
pubmed:abstractText
Circular dichroism and fluorescence measurements showed a reduced conformational order in proteins of a normal human lens when they were incubated in vitro with melittin, a bee venom peptide. Since melittin is also known to react with lipids to induce a breakdown of vesicular structure, the observed denaturation of water-soluble proteins of a human lens that developed a cataract due to multiple bee stings may be accounted for by the effects of melittin to some extent. The melittin-induced decrease of conformational order, as observed in our in-vitro studies could thus be of physiological significance.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0271-3683
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1065-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Melittin-induced conformational changes in human lens protein.
pubmed:affiliation
Division of Crystallography and Molecular Biology, Saha Institute of Nuclear Physics, Calcutta, India.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't