期刊论文详细信息
FEBS Letters
Phosphorylation of tyrosine prevents dityrosine formation in vitro
Seelos, Christian2  Gmeiner, Bernhard1 
[1] Department of Medical Chemistry, University of Vienna, Waehringerstrasse 10, A-1090 Vienna, Austria;Department of Nutrition and Biological Sciences, University of Vienna, Waehringerstrasse 10, A-1090 Vienna, Austria
关键词: Tyrosine;    Dityrosine;    Phosphotyrosine;   
DOI  :  10.1016/0014-5793(89)81130-5
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

Treatment of L-tyrosine in a peroxidase/H2O2, system results in the formation of dityrosine. However, the phosphoester derivative of tyrosine, O-phospho-L-tyrosine, was unable to form dityrosine even in mixtures with free L-tyrosine. Dephosphorylation of O-phospho-L-tyrosine by alkaline phosphatase followed by horseradish peroxidase/H2O2, treatment resulted in the formation of dityrosine. Our in vitro results indicate that phosphorylation/dephosphorylation of L-tyrosine may regulate dityrosine formation, and is supposed to play an important role in protein-protein interactions, i.e. cross-linking.

【 授权许可】

Unknown   

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