Lysosomal enzyme targeting. N-Acetylglucosaminylphosphotransferase selectively phosphorylates native lysosomal enzymes.

This publication has 28 references indexed in Scilit:

• Sialylation in vitro of purified human liver
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1981
• Enzymatic phosphorylation of lysosomal enzymes in the presence of UDP-N-acetylglucosamine. Absence of the activity in l-cell fibroblasts
  Biochemical and Biophysical Research Communications, 1981
• Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts.
  Proceedings of the National Academy of Sciences, 1977
• Chemical characterization and subunit structure of human N-acetylhexosaminidases A and B
  Biochemistry, 1976
• Lowry determination of protein in the presence of Triton X-100
  Analytical Biochemistry, 1975
• A recognition marker required for uptake of a lysosomal enzyme by cultured fibroblasts
  Biochemical and Biophysical Research Communications, 1974
• Complete Amino Acid Sequence of the Mu Heavy Chain of a Human IgM Immunoglobulin
  Science, 1973
• Chemical Structures of Pancreatic Ribonuclease and Deoxyribonuclease
  Science, 1973
• Addendum Method II: Purification of SBA by affinity chromatography
  Published by Elsevier ,1972
• Structure and Role of the Five Glycopeptides of Human IgM Immunoglobulins
  Nature New Biology, 1971