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Mutants: A Fruitful Approach to the Understanding of Asparagine-Linked Glycosylation in Eukaryotic Cells

  • James Stoll
  • Anne Rosenwald
  • Sharon S. Krag
Conference paper
Part of the NATO ASI Series book series (volume 40)

Abstract

Proteins which have glycans attached on one to six asparagine residues (N-linked glycoproteins) are important constituents of eukaryotic cells. They occur as soluble or membrane-associated components either inside or outside of cells. Secreted proteins such as thyroglobulin and immunoglobulins and intravesicular proteins such as the lysosomal glycosidases are N-linked glycoproteins. Many membrane-associated proteins found on the cell-surface are this class of glycoproteins — insulin receptor, EGF receptor, LDL receptor, and transferrin receptor, as are enzymes associated with many cellular membranes such as Na+/K+ ATPase, galactosyl transferase, sialyl transferase and HMG CoA reductase. Fibronectin and laminin, proteins found at the cell surface, also contain N-linked glycans.

Keywords

Chinese Hamster Ovary Cell Asparagine Residue Cholesteryl Oleate Glycosylation Reaction Dolichyl Phosphate 
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.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1990

Authors and Affiliations

  • James Stoll
    • 1
  • Anne Rosenwald
    • 1
  • Sharon S. Krag
    • 1
  1. 1.Department of Biochemistry School of Hygiene and Public HealthThe Johns Hopkins UniversityBaltimoreUSA

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