Linked Life Data

3409984

Source:http://linkedlifedata.com/resource/pubmed/id/3409984

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-10-7
pubmed:abstractText
Mixed disulfide between lens crystallin and glutathione has been observed in human cataracts and could be formed in vitro by thiol-disulfide exchange reaction. The glutathionyl crystallins have been reported to become partially unfolded. The present paper reports the conformational destabilization by the mixed disulfide formation in calf alpha- and gamma-II crystallin. The conformational stability was studied by the denaturants urea and guanidine hydrochloride (Gdn-HCl), and by proteolytic degradation. The denaturation curves of both urea and Gdn-HCl shift to lower denaturant concentration for crystallins of glutathione mixed disulfide. The decrease in conformational stability is estimated to be 0.22- and 0.92 kcal mol-1 for modified alpha- and gamma-II crystallin, respectively. Proteolytic digestion also shows a faster rate of degradation for the modified crystallins. These results indicate that mixed disulfide destabilizes the crystallin conformation. The destabilization may make crystallins more susceptible to changes as observed in aging lenses.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-4835
pubmed:author
pubmed:issnType
Print
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17-25
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Destabilization of lens protein conformation by glutathione mixed disulfide.
pubmed:affiliation
Howe Laboratory of Ophthalmology, Massachusetts Eye and Ear Infirmary, Department of Ophthalmology, Harvard Medical School, Boston 02114.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.