Abstract
The relationship between the two α-glucosidases is of interest since the lysosomal and microsomal β-glucuronidases are products of the same structural gene (Owens, et. al., Arch. Biochem. Biophys. 166:258, 1975) while the lysosomal, Golgi and cytosolic α-manosidases appear to be genetically distinct (Tulsiani, et.al. Fed. Proc. 35:1727, 1976). The acid (lysosomal) α-glucosidase from human liver has been purified 2400-fold and its carbohydrate composition has been determined. The Con A binding of the acid α-glucosidase is prevented by D-mannose or α-methyl-D-glucoside. At half saturation 12.5 moles of Con A are bound per mole of enzyme. The binding is demonstrable both with the purified enzyme and crude homogenates. The neutral (soluble) α-glucosidase has been specifically assayed in homogenates. In contrast to the acid glucosidase, Con A does not bind the neutral glucosidase which suggests that its carbohydrate moiety may differ from that of the acid glucosidase, if the neutral glucosidase is in fact a glycoprotein. Further, antiserum to the acid α-glucosidase inhibits its activity but in contrast has no effect on the activity of the neutral α-glucosidase. We are isolating the neutral α-glucosidase to further investigate the relationship between the two α-glucosidases.
Article PDF
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Murray, A., Townsend, R. & Nelson, T. THE “ACID AND ”NEUTRAL“ α-GLUCOSIDASES OF HUMAN LIVER. Pediatr Res 11, 460 (1977). https://doi.org/10.1203/00006450-197704000-00544
Issue Date:
DOI: https://doi.org/10.1203/00006450-197704000-00544