Cerebellar N-acetyl-beta-D-glucosaminidase: a study of the enzyme in bulk-isolated purkinje and granule cells.

Abstract

The specific activity of the lysosomal glycosidase N-acetyl-beta-D-glucosaminidase was determined in Purkinje cell bodies and granule cells isolated in bulb from cerebella of 13-, 15- and 18-day-old rats, and somewhat higher values were found for the enzyme in the Purkinje cell bodies. Although the pH profile of N-acetyl-beta-D-glucosaminidase in both neuronal types was similar, the activity in the granule cells exhibited two "pH optima". The glycosidase could be readily solubilized from both neuronal types by repeated freezing and thawing and, upon sedimentation in sucrose density gradients, the solubilized activity appeared as two distinct molecular components. The findings demonstrate the feasibility of detailed and direct comparative studies of neuron-specific patterns of enzymatic development and the excellent suitability of bulk-isolated cells for this purpose.