A rapid approach for the detection, quantification, and discovery of novel sulfenic acid or S-nitrosothiol modified proteins using a biotin-switch method.
The recent development of robust methods for the detection of proteins susceptible to S-nitrosylation (RSNO) and sulfenation (RSOH) has provided greater insight into the role of these oxidative modifications in cell signaling. These techniques, which have been termed "biotin-switch" methods, essentially use selective chemical reduction to swap an oxidative modification for a stable easily detectable biotin-tag. This allows for the rapid purification and subsequent detection of modified proteins using mass spectrometry. This chapter provides an overview of these biotin-switch methods, and explores its impact on the field of redox biology, including recent advances as well as limitations associated with this technique.
Burgoyne
Joseph R
JR
Cardiovascular Division, Department of Cardiology, King's College London, The Rayne Institute, St Thomas' Hospital, London, United Kingdom.
Eaton
Philip
P
D000818:Animals; D001710:Biotin / Q000737:chemistry*; D019411:Clinical Laboratory Techniques; D006801:Humans; D008954:Models, Biological; D010084:Oxidation-Reduction; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000032:analysis* / Q000378:metabolism*; D026403:S-Nitrosothiols / Q000378:metabolism*; D013434:Sulfenic Acids / Q000378:metabolism*; D013997:Time Factors
D011506:Proteins; D026403:S-Nitrosothiols; D013434:Sulfenic Acids; D001710:Biotin