The five fractions Pal-Pa5 each contain a single molecule identified by SDS-PAGE and the mitogenic activity present in each fraction is stable to periodate and mercaptoethanol. Mitogens in fractions Pa2-Pa5 are probably in the form of a single polypeptide chain, whereas the molecule in Pa1 appears to be a polymer of 22 kDa subunits.

In comparison with phytohemagglutinin (PHA), the polypeptide part of the PWM is remarkable for its large number of internal disulfide bridges. The compositions of the molecules in fractions Pa2-Pa5 were found to have high half-cystine values, much higher than that of the molecule in the Pal fraction.

Yokohama and colleagues have reported that the mitogens in the Pal and Pa2 fractions recognize a core NN'-diacetylchitobiose moiety in asparagine-linked sugar chains of glycoproteins, and they demonstrated the presence of receptors for these mitogens on the surface of human erythrocytes and murine lymphocytes.

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