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Purification of normal human urinary N-acetyl-beta-hexosaminidase A by affinity chromatography.


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.

SUBMITTER: Banerjee DK 

PROVIDER: S-EPMC1165192 | BioStudies | 1975-01-01

SECONDARY ACCESSION(S): 10.1042/bj1450113

REPOSITORIES: biostudies

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