Purification of the N-Acetylglucosamine-1-Phosphodiester α-N-Acetylglucosamindase from Human Lymphoblasts
Part of the
NATO ASI Series
book series (volume 74)
The G1cNAc-1-phosphodiester α-N-acetylglucosaminidase (“uncovering enzyme”) plays a key role in the intracellular targeting of lysosomal enzymes by catalyzing the removal of N-acetylglucosamine exposing mannose-6-phosphate residues on high mannose and/or hybrid oligosaccharide chains of lysosomal enzymes. The subcellular localization of the uncovering enzyme has been proposed to be associated with the cis Golgi cisternae, but no definitive evidence exists as to either its exact location or structure.
KeywordsLysosomal Enzyme Intracellular Target High Mannose Activity Fold Purify Enzyme Preparation
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
Varki A, Kornfeld S (1981) Purification and characterization of rat liver n-
N-acetylglucosaminyl phosphodiesterase. J Biol Chem 256: 9937–9943PubMedGoogle Scholar
Waheed A, Hassilik A, Von Figura K (1981) Processing of the phosphorylated recognition marker in lysosomal enzymes. J Biol Chem 256: 5717–5721PubMedGoogle Scholar
© Springer-Verlag Berlin Heidelberg 1993