Altered aspartate in Alzheimer neurofibrillary tangles.
Altered aspartate in Alzheimer neurofibrillary tangles.
复制标题
阿尔茨海默病神经原纤维缠结中天冬氨酸的改变。
DOI：
10.1007/bf00966798
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发表时间：
1992
影响因子：
4.4
通讯作者：
Frey2nd,WH
中科院分区：
文献类型：
--
作者：
Payan,IL;Chou,SJ;Fisher,GH;Man,EH;Emory,C;Frey2nd,WH
正常的蛋白质结合的1-天冬氨酰/1-天冬酰胺残基可以通过外消旋化为d-天冬氨酸或通过异构化为1-异天冬氨酰形式（其中肽链通过残基的β羧基连接）进行翻译后修饰。根据这里报道的初步结果，与阿尔茨海默氏症神经缠结制剂相关的蛋白质含有显着更多的这些修改的乙酰基残基比未受影响的蛋白质从周围的灰质或正常大脑的可比制剂。
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.