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  • Title: beta-N-acetyl-D-glucosaminidase isoenzymes from human amnionic membranes.
    Author: Orlacchio A, Emiliani C, Di Renzo GC, Cosmi EV.
    Journal: Clin Chim Acta; 1986 Sep 30; 159(3):279-89. PubMed ID: 3769215.
    Abstract:
    Two beta-N-acetylglucosaminidase isoenzymes (A and B) have been identified and purified from amnionic fetal membrane. The final specific activity of A and B isoenzymes increased 225- and 185-fold respectively by a purification scheme, which included a lyophilized extract, chromatofocusing on PBE 94, pH range 5.5 to 4.0, and affinity chromatography on p-aminophenyl-2-acetamido-2-deoxy-1-thio-beta-D-glucopyranoside covalently linked to Sepharose-4B. Different electrophoretic mobility, thermostability and different thiol group modifications of the two isoenzymes were found. Acetate was a more effective competitive inhibitor than were iodoacetamide, N-acetylglucosamine and N-acetylgalactosamine more than glucosamine and galactosamine, confirming a specific 'acetamido receptor site' for both the isoenzymes.
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