Disulfide bonds reducing reagents

Sodium hydrogen telluride, (NaTeH), prepared in situ from the reaction of tellurium powder with an aqueous ethanol solution of sodium borohydride, is an effective reducing reagent for many functionalities, such as azide, sulfoxide, disulfide, activated C=C bonds, nitroxide, and so forth. Water is a convenient solvent for these transformations.28 A variety of functional groups including aldehydes, ketones, olefins, nitroxides, and azides are also reduced by sodium hypophosphite buffer solution.29... 

Cleland (1964) showed that DTT and DTE are superior reagents in reducing disulfide bonds in proteins (see previous discussion, this section). DTT and DTE have low oxidation-reduction potential and are capable of reducing protein disulfides at concentrations far below that required with 2-mercaptoethanol. However, even these reagents have to be used in approximately 20-fold molar excess in order to get close to 100 percent reduction of a protein. 

Radiolabel 55 nmol of SASD using IODO-GEN (Thermo Fisher) and 40 pCi Na 125I for 30 seconds. Do not use chloramine-T, since termination of the iodination reaction with this reagent involves addition of a reducing agent which may cleave the disulfide bonds of the crosslinker. 

Inhibits serine proteases such as trypsin and chymotrypsin. Also inhibits cysteine proteases (reversible by reduced thiols) and mammalian acetylcholinesterase Inhibits ATPase, alkaline phosphatase and tyrosine phosphatase Reagent for maintaining -SH groups in the reduced state. Effective for reducing protein disulfide bonds prior to SDS-PAGE... 

As exemplarily shown in the case of charybdotoxin, a 37-residue peptide with three intramolecular disulfide bonds,[70] operating in redox buffer was crucial for efficient formation of the correct disulfide bonds.[71] When the reduced peptide was oxidized in 0.1 M NHtOAc buffer (pH 8.0) at 0.11 mM concentration in the presence of redox reagents (peptide/GSH/GSSG ratio of 1 60 6), the main product was the native peptide contaminated... 

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