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- W2005909719 abstract "Sulphatases B1alpha and B1beta (EC 3.1.6.1) have been prepared as apparently homogeneous proteins by chromatography on ConA-Sepharose. Both have a mol. wt. of 56 000, and E1%280nm of 17 and a turnover number of 8600 min-1 with nitrocatechol sulphate as substrate. Their amino acid compositions are identical: like sulphatase A, the sulphatases B are rich in proline and yield glucosamine on hydrolysis. They are not altered by treatment with neuraminidase. Both fractions show strong UDP-N-acetylgalactosamine 4-sulphatase activity, weak iduronate sulphatase activity, but no significant heparan N-sulphatase activity. It is suggested that the physiological activity of sulphatase B is that of the N-acetylgalactosamine 4-sulphatase which is lacking in the Maroteaux-Lamy Syndrome." @default.
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- W2005909719 date "1976-12-01" @default.
- W2005909719 modified "2023-09-23" @default.
- W2005909719 title "The sulphatase of ox liver. XX. The preparation of sulphatases B1α and B1β" @default.
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- W2005909719 doi "https://doi.org/10.1016/0005-2744(76)90193-5" @default.
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