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  • Title: Immunochemical properties of Mg erythrocytes.
    Author: Dahr W, Metaxas-Bühler M, Metaxas MN, Gallasch E.
    Journal: J Immunogenet; 1981 Apr; 8(2):79-87. PubMed ID: 6164735.
    Abstract:
    The major erythrocyte membrane (MN) sialoglycoprotein in Mg red cells was found to exhibit a slightly decreased sodium-dodecyl-sulphate polyacrylamide gel electrophoretic molecular weight and periodic and/Schiff staining intensity. Mg antigen activity was shown to be associated with this molecule. As judged from chemical modification experiments, no carbohydrate but the glycoprotein's N-terminal amino acid is involved in the Mg receptor site. The endgroup of the glycoprotein was found to leucine and studies involving Staphylococcus aureus V8 protease suggest that a glutamic acid is located at the fifth position of its peptide chain. This indicates that the Mgs gene complex evolved from a mutation of an Ns allele. An amino acido substitution or deletion at the second, third and/or fourth position(s), preventing the glycosylation of all or some of these amino acids, provides an explanation for the properties of Mg erythrocytes.
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