Abstract:
Camel lens s-crystallin/NADPH:quinone oxidoreductase activity was inhibited
by trinitrobenzene sulfonic acid (TNBS) with NADPH as an electron donor and
dichlorophenolindophenol (DCIP) as an electron acceptor in a time-independent but
concentration dependent manner. The rco of TNBS was 30 ulvl. The inhibition was
noncompetitive with respect to DCIP as deduced by Lineweavcr-Burk plots. The
estimated inhibition constant (Ki) was 35 uM.
The inhibition of s-crystallin by TNBS will give an insight into understanding
the catalytic activity of this enzyme whose function. nature of active site and
importance are yet to be fully established.