beta-N-acetyl-D-glucosaminidase isoenzymes from human amnionic membranes

Clinica Chimica Acta; International Journal of Clinical Chemistry
Aldo OrlacchioE V Cosmi

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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Citations

Jan 1, 1991·The International Journal of Biochemistry·H A BeukesR J Naude
May 17, 2002·The Journal of Veterinary Medical Science·Reeko SatoYoshihisa Naito

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