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Altered aspartate in Alzheimer neurofibrillary tangles.

作者信息

Payan I L, Chou S J, Fisher G H, Man E H, Emory C, Frey W H

机构信息

Department of Chemistry, University of Miami, Coral Gables, Florida 33124.

出版信息

Neurochem Res. 1992 Feb;17(2):187-91. doi: 10.1007/BF00966798.

Abstract

Normal protein-bound L-aspartyl/L-asparaginyl residues may undergo post-translational modification by racemization to D-aspartate, or by isomerization to the L-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.

摘要

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