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. 1987 Jun 15;244(3):801-4.
doi: 10.1042/bj2440801.

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

T Beccari  1 , C Emiliani, R Hosseini, A Orlacchio, J L Stirling
Affiliations

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

T Beccari et al. Biochem J. .

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

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