Linked Life Data

3178231

Source:http://linkedlifedata.com/resource/pubmed/id/3178231

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-11-17
pubmed:abstractText
alpha-, beta-, and gamma-crystallins have been purified from nonpathological lenses of calves. The pure proteins have been examined for nontryptophan fluorescence and fluorescent compounds have been found specifically bound to gamma 2-crystallin. The protein has been unfolded by 6 M guanidine hydrochloride (Gdn-HCl) and a separation of the fluorescent compounds has been obtained by gel chromatography in the presence of 6 M Gdn-HCl. The spectroscopic features (absorbance, fluorescence) of the protein returned to normal following removal of the chromophores. The low-molecular-weight separated fluorescent compounds have been fractionated and extracted from the Gdn-HCl solution by ethyl acetate. TLC chromatography has shown the presence of kynurenine, 3-OH-kynurenine, and free tryptophan. These data suggest that direct involvement of the intrinsic protein tryptophans in the photochemical processes leading to formation of fluorescent compounds has to be excluded. Free tryptophan and intrinsic metabolic factors are probably more relevant in determining the cataractous insult.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
61-71
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Presence of nontryptophan fluorophores specifically bound to gamma 2-crystallin.
pubmed:affiliation
Department of Biochemistry and Biophysics, University of Naples, Italy.
pubmed:publicationType
Journal Article