Linked Life Data

12054555

Source:http://linkedlifedata.com/resource/pubmed/id/12054555

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-6-10
pubmed:abstractText
alpha A-Crystallin high-molecular-weight (HMW) aggregates were prepared by preheating at 80-90 degrees C and studied using spectroscopic measurements. Conformational differences were suggested based on data of increased bis-ANS (4,4(')-dianilino-1,1(')-binaphthalene-5,5(')-disulfonic acid) and ThT (thioflavin T) fluorescence as well as increased far-UV and decreased near-UV circular dichroism (CD). These results indicated that HMW aggregated alpha-crystallin was more hydrophobic than the native alpha-crystallin, possibly resulting from partial unfolding of alpha-crystallin. The two cysteines in alpha A-crystallin were mostly oxidized in HMW aggregates. The effects of HMW aggregation on the dynamic structure were studied with fluorescence resonance energy transfer; subunit exchange became slower. These results strongly suggest that HMW alpha A-crystallin aggregates result from exposure of buried beta-pleated sheets and increased hydrophobic interaction.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
293
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7-12
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Decreased subunit exchange of heat-treated lens alpha A-crystallin.
pubmed:affiliation
Department of Ophthalmology, Center for Ophthalmic Research, Brigham and Women's Hospital, Harvard Medical School, 221 Longwood Avenue, Boston, MA 02115, USA. jliang@rics.bwh.harvard.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't