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http://dx.doi.org/10.5012/bkcs.2014.35.3.709

Mass Spectrometry Analysis of In Vitro Nitration of Carbonic Anhydrase II  

Lee, Soo Jae (Department of Applied Chemistry, College of Applied Sciences, Kyung Hee University)
Kang, Jeong Won (Department of Applied Chemistry, College of Applied Sciences, Kyung Hee University)
Cho, Kyung Cho (Department of Applied Chemistry, College of Applied Sciences, Kyung Hee University)
Kabir, Mohammad Humayun (Department of Applied Chemistry, College of Applied Sciences, Kyung Hee University)
Kim, Byungjoo (Korea Research Institute of Standards and Science)
Yim, Yong-Hyeon (Korea Research Institute of Standards and Science)
Park, Hyoung Soon (DiaTech Korea Co., Ltd)
Yi, Eugene C. (Department of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, and College of Medicine, Seoul National University)
Kim, Kwang Pyo (Department of Applied Chemistry, College of Applied Sciences, Kyung Hee University)
Publication Information
Bulletin of the Korean Chemical Society / v.35, no.3, 2014 , pp. 709-714 More about this Journal
Abstract
Protein tyrosine nitration is considered as an important indicator of nitrosative stresses and as one of the main factors for pathogenesis of inflammation and neuronal degeneration. In this study, we investigated various nitrosative modifications of bovine carbonic anhydrase II (CAII) through qualitative and semi-quantitative analysis using the combined strategy of Fourier transformation ion cyclotron resonance mass spectrometry (FT-ICR MS) and ion-trap tandem mass spectrometry (IT-MS/MS). FT-ICR MS and its spectra were used for the search of the pattern of nitrosative modifications. Identification of nitrosatively modified tyrosine sites were executed through IT-MS/MS. In addition, we also tried to infer the reason for the site-specific nitrosative modifications in CAII. In view of the above purpose, we have explored- i) the side chain accessibility, ii) the electrostatic environment originated from the acidic/basic amino acid residues neighboring to the nitrosatively modified site and iii) the existence of competing amino acid residues for nitration.
Keywords
Mass spectrometry; FT-ICR MS; High resolution MS; Nitration; Nitrosylation;
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