Abstract
We have purified the neurosteroid sulfatase (NSS) from Triton X-100 solubilized microsomes of bovine brain about 100-fold. The purified enzyme is composed of two catalytic units (MW: 57 kDa) and two regulatory units (MW: 38 kDa), making it an α 2β 2 heterotetramer, whose apparent molecular weight was 180 kDa by gel filtration in the presence of Triton X-100.
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