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Human alpha-fetoprotein (HAFP) isolated by immunoadsorbent column was shown to suppress the mitogenic response of human lymphocytes to phytomitogens, antihuman thymocyte antiserum, and the mixed lymphocyte culture. HAFP isolated from the sera and ascitic fluid of five hepatoma patients, and from fetal liver, varied in biological potency over three orders of magnitude. Extended agarose gel electrophoresis and crossed immunoelectrophoresis demonstrated three molecular species of HAFP. Quantitation of the three species revealed a correlation between the relative amount of the most negatively charged species and biological potency. Treatment of HAFP with neuraminidase to remove completely sialic acid residues did not alter the biological potency, but converted the three species to two species having slower electrophoretic mobilities. We conclude that differences in sialic acid content are only partly responsible for the microheterogeneity demonstrated by HAFP, and that variability in another charged moiety is also present. Variation in the relative proportions of the different molecular species of HAFP may be important in the regulation of its immunosuppressive properties.

Human alpha-fetoprotein as a modulator of human lymphocyte transformation: correlation of biological potency with electrophoretic variants.