THE AMINO-ACID-SEQUENCE OF THE MC-SPECIFIC MAJOR RED-CELL MEMBRANE SIALOGLYCOPROTEIN - AN INTERMEDIATE OF THE BLOOD GROUP-M-ACTIVE AND GROUP-N-ACTIVE MOLECULES

  • 1 January 1981
    • journal article
    • research article
    • Vol. 362  (3) , 363-366
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 7 residues was as follows: .**GRAPHIC**. The variant Mc apparently 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 1 and 5, respectively. The elucidation of the structure of the Mc-specific glycoprotein explains the specificity of various anti-M and anti-N reagents.