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- W1966336029 abstract "Arylsulfatase A and arylsulfatase B were purified in high yields from normal human liver by a multiple-column chromatographic procedure. The specific activity toward nitrocatechol sulfate was 4.82 μmol/min/mg for arylsulfatase A and 4.07 μmol/min/mg for arylsulfatase B with Km values of 1.8 × 10−3 and 2.9 × 10−3m, respectively. The pH optimum was found to be 5.2 for arylsulfatase A and 5.6 for arylsulfatase B. The two enzymes varied markedly in their ultraviolet absorption spectra, and the specific extinction coefficient at 280 nm was 8.56 for arylsulfatase A and 15.51 for arylsulfatase B. At pH below 4.0 and in the presence of 1% sodium dodecyl sulfate the arylsulfatase A was irreversibly converted into inactive subunits as was described for the bovine arylsulfatase A. Both arylsulfatase A and arylsulfatase B were found to have molecular weights similar to the purified ox liver enzymes." @default.
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- W1966336029 date "1975-01-01" @default.
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- W1966336029 title "Purification and some properties of soluble human liver arylsulfatases" @default.
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- W1966336029 doi "https://doi.org/10.1016/0003-9861(75)90109-5" @default.
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