Identification of β-N-acetylhexosaminidase A in mouse tissues with the fluorigenic substrate 4-methylumbelliferyl-β-N-acetylglucosamine 6-sulphate

Abstract

beta-N-Acetylhexosaminidase from mouse tissue was separated into its constituent isoenzymes on DEAE-cellulose and its activity was monitored with 4-methylumbelliferyl-beta-N-acetylglucosamine and 4-methylumbelliferyl-beta-N-acetylglucosamine 6-sulphate. Forms corresponding to the human isoenzymes A (acidic), B (basic) and an ‘intermediate’ form were present in mouse liver and spleen, whereas in kidney the B and ‘intermediate’ forms predominated, with A present only as a minor component. In brain the ‘intermediate’, A and C activities were detected. Testis had predominantly A activity, whereas epididymis, the tissue with the highest specific activity of beta-N-acetylhexosaminidase, had an abundance of the ‘intermediate’ form, but was almost entirely lacking in the A form.