We have purified the neurosteroid sulfatase (NSS) from Triton X-100 solubil
ized microsomes of bovine brain about 100-fold. The purified enzyme is comp
osed of two catalytic units (MW: 57 kDa) and two regulatory units (MW: 38 k
Da), making it an alpha(2)beta(2) heterotetramer, whose apparent molecular
weight was 180 kDa by gel filtration in the presence of Triton X-100. (C) 2
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