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: Comparison of alkal-labile oligosaccharide chains of M and N blood-group glycopeptides from human erythrocyte membrane.
    Author: Lisowska E, Duk M, Dahr W.
    Journal: Carbohydr Res; 1980 Feb; 79(1):103-13. PubMed ID: 7357568.
    Abstract:
    Alkali-borohydride degradation of M or N blood-group active, tryptic glycopeptides and glycoproteins was performed under conditions giving the reduced oligosaccharides in a yield significantly improved over that reported earlier. Degradation of desialosylated glycoproteins yielded beta-D-Galp-(1 leads to 3)-D-GalNAcol, D-GalNA-col, and Galol in a ratio of approximately 30:1:1. GalNAc was shown to be alpha-D-linked to the polypeptide chain. Degradation of the glycopeptides gave the tetrasaccharide, NeuAc-(2 leads to 3)-beta-D-Galp-(leads to 3)-[NeuAc-(2 leads to 6)]-D-GalNAcol, and two trisaccharides, NeuAc-(2 leads to 3)-beta-D-Galp-(1 leads to 3)-D-GalNAcol and beta-D-Galp-(1 leads to 3)-[NeuAc-(2 leads to 6)]-D-GalNAcol, in a molar ratio of approximately 8:3:1. These oligosaccharides were accompanied by minor amounts of unidentified compounds showing identical electrophoretic mobility when derived from M and N glycopeptides. During isolation of the reduced oligosaccharides, the release of sialic acid did not exceed 5.5%, indicating that only a part of the trisaccharide portion might have arisen as a result of desialosylation of the tetrasaccharide. No differences between the degradation products derived from M and N glycoproteins were found, and the presence of significant amounts of larger, alkali-labile oligosaccharides was not observed.
    [Abstract] [Full Text] [Related] [New Search]