Structural analysis of the asparagine-linked oligosaccharides from three lysosomal enzymes of Dictyostelium discoideum. Evidence for an unusual acid-stable phosphodiester.-Reference-Cited by-同舟云学术

Structural analysis of the asparagine-linked oligosaccharides from three lysosomal enzymes of Dictyostelium discoideum. Evidence for an unusual acid-stable phosphodiester.

Published:1983-12 Issue:24 Volume:258 Page:14874-14879
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Freeze H H,Yeh R,Miller A L,Kornfeld S

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference24 articles.

1. Secretion of Lysosomal enzymes in the cellular slime mold, Dictyostelium discoideum.

2. Enzyme synthesis in myxamoebae of the cellular slime mould Dictyostelium discoideum during growth in axenic culture

3. Acid hydrolases from Dictyostelium discoideum contain phosphomannosyl recognition markers.

4. Binding of phosphorylated oligosaccharides to immobilized phosphomannosyl receptors.

5. The spectrum of anionic oligosaccharides released by endo-beta-N-acetylglucosaminidase H from glycoproteins. Structural studies and interactions with the phosphomannosyl receptor.

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