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N-nitrosations of basic amino acid residues in polypeptide
Wu-Nan Kuo1, Dynisha Ivy, Luvina Guruvadoo
1Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida 32114, USA. kuow@cookman.edu
Frontiers in Bioscience : a Journal and Virtual Library
|September 9, 2004
Summary
N-nitrosation of amino acids in polypeptides was observed, affecting lysine, arginine, and histidine. Histones H2A and H2B showed increased N-nitroso immunoreactivity, indicating nitrosative stress in proteins.
Area of Science:
- Biochemistry
- Proteomics
- Chemical Biology
Background:
- Nitrosative stress can alter protein structure and function.
- Amino acids like lysine, arginine, and histidine are susceptible to chemical modifications.
Purpose of the Study:
- To investigate the N-nitrosation of specific amino acid residues in polypeptides.
- To assess the impact of reactive or degraded nitrogen species on protein modification.
Main Methods:
- Electrophoretic analysis of polypeptide products.
- Western blot analysis for N-nitroso immunoreactivity detection.
Main Results:
- Observed changes in electrophoretic patterns of polypeptides containing lysine, arginine, and histidine.
- Confirmed N-nitrosation of the epsilon-amino group of lysine, guanido group of arginine, and imidazole group of histidine.
- Detected increased N-nitroso immunoreactivity in histones H2A and H2B.
Conclusions:
- Reactive or degraded nitrogen species can cause N-nitrosation of key amino acid residues in proteins.
- Histones H2A and H2B are susceptible to N-nitrosation, suggesting potential roles in nitrosative stress responses.