N-Acetyl-beta-hexosaminidase A was purified 1000-fold from human urine by chromatography on DEAE-Sephadex followed by concanavalin A--Sepharose affinity chromatography. The optimal pH range was 4.4--4.5 for both the N-acetylglucosamine and N-acetylgalactosamine derivatives. The Km values were 0.51 mM and 0.28 mM respectively for the N-acetylglucosamine and N-acetylgalactosamine derivatives. The glycoprotein nature of the urinary enzyme was established by its affinity towards concanavalin A as well as by the presence of sialic acid, galactose, glucose, mannose and hexosamines in the molecule.
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Research Article| January 01 1975
Purification of normal human urinary N-acetyl-β-hexosaminidase A by affinity chromatography
Biochem J (1975) 145 (1): 113–118.
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D K Banerjee, D Basu; Purification of normal human urinary N-acetyl-β-hexosaminidase A by affinity chromatography. Biochem J 1 January 1975; 145 (1): 113–118. doi: https://doi.org/10.1042/bj1450113
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