Open AccessHuman α‐ N ‐Acetylglucosaminidase
Author(s) -
FIGURA Kurt
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11908.x
Subject(s) - chemistry , enzyme , dermatan sulfate , polyacrylamide gel electrophoresis , thiol , gel electrophoresis , sodium dodecyl sulfate , reagent , chromatography , biochemistry , capillary electrophoresis , heparan sulfate , sodium , heparin , organic chemistry
α‐ N ‐Acetylglucosaminidase was purified from human urine to a state of apparent homogeneity. α‐ N ‐Acetylglucosaminidase is a glycoprotein with an extensive charge heterogeneity. The molecular weight determined by gel filtation is 307 000. Polyacrylamide gel electrophoresis in the absence and presence of sodium dodecyl sulfate indicates molecular weight heterogeneity of isocharged forms of the purified enzyme. The enzyme has a pH optimum of 4.5 ± 0.3 and K m and V values of 0.14–0.74 mM, and 1.04–3.68 μmol mg −1 min −1 for three ary1 2‐acetamido‐2‐deoxy‐α‐ D ‐glucosides and UDP‐ N ‐acetylglucosamine. Heparan sulfate, heparin and dermatan sulfate are competitive inhibitors. The enzyme is inhibited by Hg 2+ and Cu 2+ . ‐SH‐protective reagents and thiol reagents have no effect on the enzyme activity. Heating at 65°C and pH values below 5 inactivate the enzyme rapidly.