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Altered aspartate in Alzheimer neurofibrillary tangles
Authors:Iris L. Payan  Shou-Jian Chou  George H. Fisher  Eugene H. Man  Carolyn Emory  William H. Frey II
Affiliation:(1) Department of Chemistry, University of Miami, 33124 Coral Gables, Florida;(2) Department of Chemistry, Barry University, 11300 NE 2nd Ave., 33161 Miami Shores, Florida;(3) Ramsey Clinic, St. Paul-Ramsey Medical Center, Alzheimer's Treatment and Research Center, 55101 St. Paul, Minnesota
Abstract:Normal protein-boundl-aspartyl/l-asparaginyl residues may undergo post-translational modification by racemization tod-aspartate, or by isomerization to thel-isoaspartyl form in which the peptide chain links through the beta carboxyl group of the residue. Based on preliminary results reported here, proteins associated with Alzheimer neurofibrillary tangle preparations contain a significantly greater number of these modified aspartyl residues than the unaffected proteins from the surrounding gray matter or in comparable preparations from normal brains.
Keywords:  font-variant:small-caps"  >d-Aspartate (D-Asp)    font-variant:small-caps"  >l-isoaspartate (L-isoAsp)  Alzheimer's disease  human brain  protein carboxyl methyltransferase (PCM)
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