1. Tyrosine aminotransferase from guinea-pig liver is inactivated at neutral pH by a factor localized in the microsomal fraction. The inactivation, independent of exogenous L-cysteine, is rapidly reversed by addition of dithiothreitol. 2. The effects of physiological reducing agents on the enzyme inactivation were investigated. L-Cysteine and L-cysteamine enhance the inactivation rate of the en...

An enzymatic method involving a protease (pronase) for the elimination of interference factors in the latex test for cryptococcal antigen was developed and compared with dithiothreitol treatment. The two were equivalent in their ability to remove interference factors; however, the enzymatic method generally yielded higher titers. The method is simple, requires only 20 min, and makes the latex t...

A highly selective ratiometric fluorescent probe, which contains an aminonaphthalimide fluorophore and a self-immolative spacer for 1,4-dithiothreitol (DTT) detection was designed and synthesized. The probe displays a 66 nm red-shift of fluorescence emission and the color changes from colorless to jade-green upon reaction with DTT. These properties are mechanistically ascribed to the strong red...

The synthesis and characterization of the first examples of singly and doubly fused expanded porphyrins containing dithienothiophene (DTT) cores are reported.

In this study, we demonstrate a non-enzymatic method for hydrolytic peptide bond cleavage, applied to the removal of an affinity tag from a recombinant fusion protein, SPI2-SRHWAP-His(6). This method is based on a highly specific Ni(II) reaction with (S/T)XHZ peptide sequences. It can be applied for the protein attached to an affinity column or to the unbound protein in solution. We studied the...