Mass spectrometric analysis of asparagine deamidation and aspartate isomerization in polypeptides.

Mass spectrometric analysis of asparagine deamidation and aspartate isomerization in polypeptides.
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DOI:
10.1002/elps.201000027
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发表时间:
2010-06
期刊:
影响因子:
2.9
通讯作者:
Zubarev, Roman A.
Zubarev, Roman A.
中科院分区:
生物学3区
文献类型:
--
作者:
Yang, Hongqian;Zubarev, Roman A.

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蛋白质和肽中最常见的修饰之一是天冬酰胺的脱酰胺,这是一种自发的非酶反应,导致L、d -琥珀酰氨基基、L、d -天冬氨酸和L、d -异天冬氨酸形式的混合物,其中L-异天冬氨酸占主导地位。L-Asp的自发异构化产生相同的产物。在体内,这些不寻常形式的天冬氨酸被PIMT酶修复,异构化和修复之间的平衡影响生物体生理。该天平的质谱分析包括异构体分离、iso-Asp/Asp定量和iso-Asp位点鉴定。本文综述了与这些步骤相关的问题,并讨论了高通量iso-Asp分析的前景。
One of the most frequent modifications in proteins and peptides is the deamidation of asparagine, a spontaneous non-enzymatic reaction leading to a mixture of ***L,D-succinimidyl, L,D-aspartyl, and L,D-isoaspartyl forms, with L-isoaspartyl dominating. Spontaneous isomerization of L-Asp yields the same products. In vivo, these unusual forms of aspartate are repaired by the PIMT enzyme, with the balance between isomerization and repair affecting the organism physiology. Mass spectrometric analysis of this balance involves isomer separation, iso-Asp/Asp quantification and iso-Asp site identification. This review highlights the issues associated with these steps and discusses the prospects of high-throughput iso-Asp analysis.
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