Dithiothreitol is extensively used in protein analysis, especially to reduce disulfide bonds. Its reducing potential is recognized by the landmark study of Cleland (Cleland, 1964). It is also known as Cleland reagents. Its low redox potential (-0.33 at pH 7.0) makes it an ideal reagent to maintain Monothiols in a reduced state. Unlike β-mercaptoethanol, it does not have a strong smell. Moreover, DTT is seven times more effective than β-mercaptoethanol.
- Cleland, 1964. Dithiothreitol, a New Protective Reagent for SH Groups. Biochemistry. 3, 480-482. PMID-14192894; Full-Text Link: ACS Publications
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