Ochratoxin A−BSA conjugate from Aspergillus ochraceus has been used in carbonate-bicarbonate buffer to coat the high-affinity 96-well polystyrene plates for indirect competitive enzyme-linked immunosorbent assay. It has also been used as a standard in the determination of ochratoxin A in serum by capillary electrophoresis with laser-induced fluorescence detection (CE-LIF).
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Ochratoxin A (OTA) is a mycotoxin that is the most toxic among the other ochratoxins. It is produced by Aspergillus carbonarius, A. ochraceus, and Penicillium verrucosum. OTA acts as a major food contaminant and is considered nephrotoxic, teratogenic, neurotoxic, hepatotoxic, and immunotoxic. OTA is known to elevate oxidative stress at a cellular level.
The mycotoxin ochratoxin A is a potent inhibitor of the protein biosynthesis and known to be cytotoxic in nanomolar concentrations. In order to investigate the relationship between stereochemistry and cytotoxicity of this compound, all four ochratoxin A stereoisomers have been
The cysteinyl transferase mycothiol ligase, or MshC, catalyzes the fourth step in the biosynthesis of the small molecular weight thiol mycothiol. MshC is essential for growth of Mycobacterium tuberculosis. Two groups of known aminoacyl tRNA synthetase inhibitors were evaluated for
The Journal of biological chemistry, 282(33), 23841-23853 (2007-06-08)
Organic anion transporters (OATs, SLC22) interact with a remarkably diverse array of endogenous and exogenous organic anions. However, little is known about the structural features that determine their substrate selectivity. We examined the substrate binding preferences and transport function of
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