These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: [Chemical galactosylation of acid alpha-glucosidase to provide directed transport of the enzyme into lysosomes of liver parenchymal cells].
    Author: Belen'kiĭ DM.
    Journal: Vopr Med Khim; 1987; 33(5):15-20. PubMed ID: 2825427.
    Abstract:
    Chemical galactosylation of human liver tissue lysosomal alpha-glucosidase was carried out. As a result of the modification some physicochemical properties of the enzyme were altered, while its stability and catalytic activity were maintained. An ability of the galactosylated alpha-glucosidase to interact with asialoglycoprotein receptor from mice liver tissue was studied in vitro. The reaction required Ca2+. A specific inhibitor of the receptor, N-acetyl galactosamine, as well as high concentrations of native glycoproteins and neoglycoproteins containing terminal galactose inhibited the receptor binding of the 125I-galactosylated alpha-glucosidase. Native alpha-glucosidase was not bound with the receptor. Antireceptor antibodies inhibited similarly binding of both native ligand, asialoorosomucoid and the galactosylated alpha-glucosidase. These data on specific interaction between the galactosylated form of alpha-glucosidase and asialoglycoprotein receptor are discussed in connection with the problem of directed transport of the enzyme into liver parenchymatous cells by means of receptor-dependent endocytosis, which may be of importance in development of enzymotherapy of hereditary lysosomal enzymopathies.
    [Abstract] [Full Text] [Related] [New Search]