## p-Iodoethyhrifluoroacetamide was prepared and evaluated for use in the aminoethylation of sulfhydryl groups in proteins. Lysozyme, ribonuclease A, chymotrypsinogen A, and soybean trypsin inhibitor were reduced using dithiothreitol in 6 M guanidine hydrochloride. The reduced proteins were then t
5-Nitrosothio-2-nitrobenzoate: A Reagent for the Nitrosation of Thiol Groups in Proteins
β Scribed by Matthew S. Studebaker; Hao Zhang; Gary E. Means
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 111 KB
- Volume
- 237
- Category
- Article
- ISSN
- 0003-2697
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## Abstract For Abstract see ChemInform Abstract in Full Text.
The chloroamide compound 1,3,4,6-tetrachloro-3a, 6a-diphenylglycoluril is a useful solid-phase reagent for the oxidative removal of sulfhydryl groups from solution. The reaction with dithiothreitol is rapid and first order (/robs = 0.3 min-I). Titration of dithiothreitol with chloroglycoluril shows
The use of 1 -fluoro-2,4-dinitrobenzene (FDNB) as a probe for the presence of hydrodisulfide groups in proteins is described. The technique involves derivatimtion of the protein with FDNB and subsequent treatment with dithiothreitol (DTT). The 2,4dinitrothiophenol (DNTP) released from the PDNB-deri