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

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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-methyl-umbelliferyl-.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.

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