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The N-terminal structures of the Miltenberger (Mi-) blood group class I and II specific human MN erythrocyte membrane sialoglycoproteins were determined by manual sequencing of tryptic glycopeptides and various secondary fragments. The Mi-I and Mi-II active glycoproteins were found to exhibit a threonine leads to methionine and threonine leads to lysine exchange, respectively, at position 28 which prevents N-glycosylation of asparagine 26. Due to the absence of the N-glycosidic oligosaccharide chain, the monomeric form of the Mi-I and Mi-II specific glycoproteins possesses a slightly increased sodium dodecyl sulfate/polyacrylamide gel electrophoretic mobility, in comparison to its normal counterpart. Serological studies suggest that antibodies, specific for Mi-I or Mi-II red cells, react with the structurally altered region of the MN glycoprotein.
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