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

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 lymphoblastic leukaemia. Intermediate forms in these samples had no activity towards 4-methylumbelliferyl beta-N-acetylglucosaminide 6-sulphate, indicating that they lack alpha-subunits.