DTT is frequently used to reduce the disulfide bonds of
proteins and, more generally, to prevent intramolecular and
intermolecular disulfide bonds from forming between cysteine residues of
proteins.DTT is less pungent and is less toxic than 2-mercaptoethanol.
Typically, a seven fold lower concentration of DTT (100 mM) is needed
than is used for 2-mercaptoethanol (5% v/v, 700 mM).
Synonym:
Threo-1,4-dimercaptobutane-2,3-diol
DL-Threo-1,4-dimercapto-2,3-butanediol OR
,4-Dithio-DL-threitol
±-Threo-1,4-dimercapto-2,3-butanediol OR Cleland's
reagent OR Reductacryl
Molecular Formula:
C4H10O2S2
Reduction of a typical disulfide bond by DTT via two
sequential thiol-disulfide exchange reactions
References
-
Cleland, W.W. (April 1964). "Dithiothreitol, A New Protective Reagent for SH
Groups".
Biochemistry
3: 480–2.
-
Ruegg UT and Rudinger J. (1977) "Cleavage of disulfide bonds in
proteins", Methods Enzymol., 47, 111.