Abstract
The I antigen appears on human cells in the postnatal period, by addition of N-acetyllactosamine (beta 1-6) branching to the fetal i antigen structure, which is specified by linear oligo N-acetyllactosamine (beta 1-3) chain. Concurrently with the I antigen appearance on adult human erythrocytes most human sera exhibit low levels of anti-I agglutinins. These antibodies induce hemagglutination mainly at low temperatures (4 degrees C) and scantly at body temperature. Therefore they were named "cold agglutinins". We have used these antibodies and several hemagglutinating galactophilic animal, plant, and microbial lectins that also react with the I antigen, to study whether the cold-favored agglutination of the I antigen-bearing cells is a peculiar property of the anti-I antibodies or a special trait of that antigen. It has been found that the interactions of all of the examined lectins, irrespective of their source, with the adult human erythrocytes significantly increased at 4 degrees C, in contrast to those of the same cells with diverse I-insensitive antibodies and lectins, which were significantly higher at room temperature.
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