ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
: Sulfhydryl oxidase (SOX) was purified after extraction and the contaminating catalase activity was completely eliminated in the last chromatography step. A yield of 25% was obtained with a purification factor higher than 300. The isoelectric point was 3.7 and the molecular weight 110 kDa. SOX exhibited an optimal activity at pH 5.6 and its efficiency (Vmapp/Kmapp) increased from pH 4.5 to 6.5. At pH 5.6, the Kmappvalues were 0.5, 2.5, 10.5, 110, and 450 mM for GSH, cysteine, g-glu-cys, dithiothreitol, and homocysteine, respectively, and the Vmappvalues represented 2, 34, 24, and 44% of the VmaPPvalue found for GSH, respectively. Cys-gly was not oxidized by SOX. In the presence of GSH, SOX is able to catalyze the oxidation of cysteine and cys-gly at a significant rate.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.2002.tb09494.x
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