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: The amino acid sequence of the Mc-specific major red cell membrane sialoglycoprotein--an intermediate of the blood group M- and N-active molecules.
    Author: Dahr W, Kordowicz M, Beyreuther K, Krüger J.
    Journal: Hoppe Seylers Z Physiol Chem; 1981 Mar; 362(3):363-6. PubMed ID: 7227981.
    Abstract:
    The sequence and glycosylation of the N-terminal 12 amino acids of the blood group Mc-specific major erythrocyte (MN) membrane sialoglycoprotein was determined by analyses of aminoterminal tryptic and secondary V8 protease peptides from McM erythrocytes. As predicted previously, the sequence of the N-terminal seven residues was found to be: Ser-+Ser-+Thr-+Thr-Glu-Val-Ala-(+ = glycosylation). This suggests that the variant Mc represents the evolutionary link between the blood group M- and N-specific glycoproteins, which possess Ser or Leu and Gly or Glu at the positions one and five, respectively. The elucidation of the structure of the Mc-specific glycoprotein explains the specificity of various anti-M and anti-N reagents.
    [Abstract] [Full Text] [Related] [New Search]