Linked Life Data

9367870

Source:http://linkedlifedata.com/resource/pubmed/id/9367870

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-12-12
pubmed:abstractText
A new cleavage site, which is a post-translational modification, was found between residues His-154 and Ala-155 in alpha A-crystallin from the aged human lens. After trypsin digestion of alpha A-crystallin two peptides that include Asp-151 were obtained and have remarkable differences. That is, the stereo-configuration of the Asp-151 in the normal length peptide was predominately inverted to the D-isomer of beta-aspartyl form (D/L of 5.7). However, the stereoconfiguration of the Asp-151 in the cleavage peptide, that lacks the sequence following Ala-155 to the C-terminus, remained predominately in the L-isomer form as indicated by a D/L value of 0.3. The results suggest that the secondary structure in the region of Ala-155 to the C-terminus may constitute a field that causes the inversion of the Asp-151 to the D-isomer form. Since this kind of cleavage was not found in alpha A-crystallin from young lens, the cleavage between His-154 and Ala-155 is probably the result of aging.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
239
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
918-23
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The conformation formed by the domain after alanine-155 induces inversion of aspartic acid-151 in alpha A-crystallin from aged human lenses.
pubmed:affiliation
Precursory Research for Embryonic Science and Technology (PRESTO), Japan Science and Technology Corporation (JST), Ibaraki.
pubmed:publicationType
Journal Article