Intermediate forms of human β-N-acetylhexosaminidase lack activity towards 4-methylumbelliferyl β-N-acetylglucosaminide 6-sulphate

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Abstract
4-Methylumbelliferyl .beta.-N-acetylglucosaminide-6-sulphate was purified from a mixture containing its unsulphated precursor. The substrate was used to test for the presence of functional .alpha.-subunits in ''intermediate'' forms of human .beta.-N-acetylhexosaminidase in samples of normal and pregnancy serum and in extracts of placenta and lymphocytes from a patient with common acute lymhoblastic leukaemia. Intermediate forms in these samples had no activity towards 4-methylumbelliferyl .beta.-N-acetylglucosaminide-6-sulphate, indicating that they lack .alpha.-subunits.