Abstract
The sulfoxide reduction of sulindac (cis-5-fluoro-2-methyl-1-[p-(methylsulfinyl)-benzylidenyl]indene-3-acetic acid), an anti-inflammatory agent, was demonstrated in vitro by cell-free preparations of guinea pig liver. The sulfoxide reductase activity was located in both fractions of microsomes and 105000X g supernatant. The microsomal reductase was NADPH- or NADH-dependent, and required the factor present in the soluble fraction for its activity. The factor was heat-labile and non-dialyzable. Furthermore, a partial purification of the microsomal NADPH-cytochrome c reductase resulted in a paralleled increase of the sulfoxide reductase activity. The present observations suggest that the soluble factor described above functions as an electron transfer component coupled with NADPH-cytochrome c reductase.
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