Studies of the reactivity of the various anti-human blood group N reagents with isolated human blood group M and N antigens and smaller molecules revealed besides the expected interaction with N antigens that M antigens inhibited all rabbit anti-N sera, Vicia graminea extract and most human anti-N sera. Mild acid hydrolysis of M antigens, which released sialic acid only, led to a large increase or de novo appearance of this inhibitory capacity. The partially hydrolyzed M antigens became temporarily indistinguishable from N antigens, indicating that the product of the N gene is the immediate precursor of the product of the M gene and that the allele to the M gene is an amorph. In the NM biosynthetic pathway, the U'c/a-reactive structure seems to precede the N-specific molecule. Uncovering of N-specific structures paralleled the appearance of terminal β-D-galactopyranosyl structures; their exposure to β-galactosidase resulted in destruction of N specificity. Galactose and some β-D-galactopyranosyl derivatives inhibited the N erythrocyte agglutination by some anti-N sera. Ganglioside I and ‘asialoganglioside’ were inhibitors of anti-N reagents and anti-ganglioside serum reacted preferentially with human blood group N antigens.
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