详细记录  
题名: Proteomic methods for analysis of S-nitrosation
作者:Nicholas J. Kettenhofen, Katarzyna A. Broniowska, Agnes Keszler, Yanhong Zhang and Neil Hogg
来源:Journal of Chromatography B[IF=----], In Press, Corrected Proof, Available online 25 February 2007,
URL :http://dx.doi.org/10.1016/j.jchromb.2007.02.035
日期:070415
摘要: Nicholas J. Kettenhofena, Katarzyna A. Broniowskaa, Agnes Keszlera, Yanhong Zhanga and Neil Hogg, a,

aDepartment of Biophysics and Free Radical Research Center, Medical College of Wisconsin, Milwaukee, WI 53226, USA

Received 14 August 2006; accepted 5 February 2007. Available online 25 February 2007.

Summary

This review discusses proteomic methods to detect and identify S-nitrosated proteins. Protein S-nitrosation, the post-translational modification of thiol residues to form S-nitrosothiols, has been suggested to be a mechanism of cellular redox signaling by which nitric oxide can alter cellular function through modification of protein thiol residues. It has become apparent that methods that will detect and identify low levels of S-nitrosated protein in complex protein mixtures are required in order to fully appreciate the range, extent and selectivity of this modification in both physiological and pathological conditions. While many advances have been made in the detection of either total cellular S-nitrosation or individual S-nitrosothiols, proteomic methods for the detection of S-nitrosation are in relative infancy. This review will discuss the major methods that have been used for the proteomic analysis of protein S-nitrosation and discuss the pros and cons of this methodology. 8ku 3:

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