ALTERED ASPARTATE IN ALZHEIMER NEUROFIBRILLARY TANGLES

被引:35
作者
PAYAN, IL
CHOU, SJ
FISHER, GH
MAN, EH
EMORY, C
FREY, WH
机构
[1] BARRY UNIV, DEPT CHEM, 11300 NE 2ND AVE, MIAMI, FL 33161 USA
[2] UNIV MIAMI, DEPT CHEM, CORAL GABLES, FL 33124 USA
[3] ST PAUL RAMSEY MED CTR, RAMSEY CLIN, ALZHEIMERS TREATMENT & RES CTR, ST PAUL, MN 55101 USA
关键词
D-ASPARTATE (D-ASP); L-ISOASPARTATE (L-ISOASP); ALZHEIMERS DISEASE; HUMAN BRAIN; PROTEIN CARBOXYL METHYLTRANSFERASE (PCM);
D O I
10.1007/BF00966798
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:187 / 191
页数:5
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