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Title: Purification of normal human urinary N-acetyl-beta-hexosaminidase A by affinity chromatography. Author: Banerjee DK, Basu D. Journal: Biochem J; 1975 Jan; 145(1):113-8. PubMed ID: 242317. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]