Abstract
The present study represents an initial investigative effort to purify sulfide oxidase from rat liver. Two methods to determine sulfide oxidase activity have been established and both are based on measuring substrate disappearance of sulfide. Both methylene blue and ion selective electrode methods are simple, convenient and accurate. Ultimately the methylene blue method was preferred over the ion selective electrodes method due to its greater sensitivity and smaller size sample requirements. Sulfide oxidase from rat liver has been isolated and purified by means of ammonium sulfate fractionation, anion-exchange chromatography, and size exclusion chromatography. The use of 80% saturation with ammonium sulfate at pH 7.2 provided an initial precipitation of sulfide oxidase, provided an initial precipitation of sulfide oxidase, and after chromatographic procedures a 21 fold purification of the enzyme was obtained.
Pu, Lixia (1994). Purification of sulfide oxidase from rat liver. Master's thesis, Texas A&M University. Available electronically from
https : / /hdl .handle .net /1969 .1 /ETD -TAMU -1994 -THESIS -P976.