Ontology highlight
ABSTRACT:
SUBMITTER: Shimizu K
PROVIDER: S-EPMC3398496 | biostudies-literature | 2012
REPOSITORIES: biostudies-literature
Molecular vision 20120704
<h4>Purpose</h4>The aspartyl (Asp) residues 58 and 151 in αA-crystallin, and Asp36 and Asp62 in αB-crystallin in human lenses are known to be highly isomerized with aging. We investigate structural environments of these isomerizable aspartyl residues in α-crystallins of human lenses.<h4>Methods</h4>To perform limited proteolysis experiments of purified human αA- and αB-crystallins, endoproteinase Asp-N (EC 3.4.24.33), which selectively cleaves the peptide bonds at the amino side of aspartyl and ...[more]