WebJan 15, 2009 · The focus of this review is the biotin-switch technique (BST), which has become a mainstay assay for detecting S-nitrosylated proteins in complex biological … Webunstable to be detected by mass spectrometry. Instead, a biotin-switch technique (BST) was used to convert unstable cysteine adducts to stable biotin-cysteine adducts, and …
Assessment and Application of the Biotin Switch …
WebMar 30, 2024 · The biotin switch technique for specifically labeling S-nitrosylated proteins opened the way to proteomic identification of these modifications. Since then, several variations and adaptations of the original method have been applied. WebMay 14, 2013 · These studies were based on the biotin switch technique (BST), which was the first assay designed to detect S-nitrosylated (SNO) proteins from cells and tissues. BST is a three-step method to convert SNO cysteines into biotinylated cysteine residues that easily be detected using streptavidin or a specific antibody ( Jaffrey and Snyder, 2001 ). green mountain coffee packets
Methods for Algal Protein Isolation and Proteome Analysis
WebMar 30, 2024 · The biotin switch technique for specifically labeling S-nitrosylated proteins opened the way to proteomic identification of these modifications. Since then, several … WebProtein Modifications and Biotin Switch Technique—Pro-teins/lysates were treated with the indicated concentrations of H 2 O 2, diamide, glutathione disulfide (GSSG), or … WebJan 28, 2014 · To globally and quantitatively analyze NO-induced protein S-nitrosylation, the sensitive gel-based proteomic method, termed NitroDIGE, was developed by combining two-dimensional differential in-gel electrophoresis (2-D DIGE) with the modified biotin switch technique (BST) using fluorescence-tagged CyDye™ thiol reactive agents to label S ... flying together sign in