IMMUNOCHEMICAL PROPERTIES OF Mg ERYTHROCYTES

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 acid/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 fitth position of its peptide chain. This indicates that the Mgs gene complex evolved from a mutation of an Ns allele. An amino acid 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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