97512-84-0Relevant articles and documents
Compositions and methods for detecting S-nitrosylation and S-sulfinylation
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Page/Page column 5; 15; 16; 27; 28, (2019/09/23)
The present invention relates to methods for detecting protein S-sulfinylation and S-sulfinylation within thiol groups in proteins, metabolites, or materials.
Conversion of S-phenylsulfonylcysteine residues to mixed disulfides at pH 4.0: Utility in protein thiol blocking and in protein-S-nitrosothiol detection
Reeves,Joshi,Campanello,Hilmer,Chetia,Vance,Reinschmidt,Miller,Giedroc,Dratz,Singel,Grieco
, p. 7942 - 7956 (2015/02/18)
A three step protocol for protein S-nitrosothiol conversion to fluorescent mixed disulfides with purified proteins, referred to as the thiosulfonate switch, is explored which involves: (1) thiol blocking at pH 4.0 using S-phenylsulfonylcysteine (SPSC); (2) trapping of protein S-nitrosothiols as their S-phenylsulfonylcysteines employing sodium benzenesulfinate; and (3) tagging the protein thiosulfonate with a fluorescent rhodamine based probe bearing a reactive thiol (Rhod-SH), which forms a mixed disulfide between the probe and the formerly S-nitrosated cysteine residue. S-Nitrosated bovine serum albumin and the S-nitrosated C-terminally truncated form of AdhR-SH (alcohol dehydrogenase regulator) designated as AdhR-SNO were selectively labelled by the thiosulfonate switch both individually and in protein mixtures containing free thiols. This protocol features the facile reaction of thiols with S-phenylsulfonylcysteines forming mixed disulfides at mild acidic pH (pH = 4.0) in both the initial blocking step as well as in the conversion of protein-S-sulfonylcysteines to form stable fluorescent disulfides. Labelling was monitored by TOF-MS and gel electrophoresis. Proteolysis and peptide analysis of the resulting digest identified the cysteine residues containing mixed disulfides bearing the fluorescent probe, Rhod-SH.
Thiosulphonate derivatives of amino acids
Hart,Vine,Walden
, p. 3879 - 3882 (2007/10/02)
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