Human liver glucuronate 2-sulphatase. Purification, characterization and catalytic properties
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منابع مشابه
Human liver N-acetylglucosamine-6-sulphate sulphatase. Purification and characterization.
Human N-acetylglucosamine-6-sulphate sulphatase was purified at least 50,000-fold to homogeneity in 78% yield from liver with a simple three-step four-column procedure, which consists of a concanavalin A-Sepharose/Blue A-agarose coupled step, chromatofocusing and Cu2+-chelating Sepharose chromatography. In all, four forms were isolated and partially characterized. Forms A and B, both with a pI ...
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The optimization of the assay conditions to detect glucuronate-2-sulphatase (GS) activity present in cultured human skin fibroblast homogenates towards a heparin-derived disaccharide substrate O-(beta-D-glucuronic acid 2-sulphate)-(1----4)-D-O-2,5-anhydro[l-3H]mannitol 6-sulphate (GSMS) has shown that a complex relationship exists between pH, buffer composition, ionic strength and the influence...
متن کاملHuman liver N-acetylglucosamine-6-sulphate sulphatase. Catalytic properties.
Kinetic parameters (Km and kcat.) of the two major forms (A and B) and a minor form (C) of human liver N-acetylglucosamine-6-sulphate sulphatase [Freeman, Clements & Hopwood (1987) Biochem. J. 246, 347-354] were determined with a variety of substrates matching structural aspects of the physiological substrates in vivo, namely heparin, heparan sulphate and keratan sulphate. Enzyme activity is hi...
متن کاملPurification, characterization and catalytic properties
Human glucuronate 2-sulphatase (GAS), which is involved in the degradation of the glycosaminoglycans heparan sulphate and chondroitin 6-sulphate, was purified almost 2000000-fold to homogeneity in 8 0 yield from liver with a four-step six-column procedure, which consists of a concanavalin A-Sepharose/Blue A-agarose coupled step, a DEAE-Sephacel/octyl-Sepharose coupled step, CM-Sepharose chromat...
متن کاملThe sulphatase of ox liver. II. The purification and properties of sulphatase A.
The first paper of this series (Roy, 1953) reported the presence of two distinct fractions exhibiting sulphatase activity in an aqueous extract of an acetone powder of ox liver, and gave preliminary data on the properties of the two crude enzymes, which were separated by fractional precipitation with acetone. The present paper describes the further purification and properties of fraction A, now...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1989
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2590209