Serum and fecal specimens were collected from vaccinees receiving Sabin vaccine. Whey was separated from mother's milk collected from those who received Salk vaccine at their late pregnancy. Each specimen was tested for antibody to poliovirus type 2 (MEF 1) and the antibody-positive specimens were pooled separately with respect to serum, whey and stool extract. From each of three pools, the globulin fraction was precipitated at half saturation of (NH
4)
2SO
4. IgG/IgA ratios of globulin fractions from serum, stool and whey were 12.53, 4.06, and 0.76, respectively, but they showed no distinction in kinetics and in avidity of the neutralizing antibody for the poliovirus. The neutralization by each of the globulin fractions followed the first order reaction. The salting-out globulin fractions were subjected to Geon 72S block electrophoresis and to step-wise elution with phosphate buffers of pH 7.5, 6.4, and 4.7 through a DEAE-cellulose column. The elutes were pooled into Fr. I, Fr. II, and Fr. III at three peaks in optical density at 280mμ. Whey Fr. II showed two peaks, Fr. II-1 and Fr. II-2, and the latter was found by ultracentrifugal analysis to contain 11S secretory IgA exclusively. Stool Fr. II was proved by immunophoretic and thin-layer chromatographic analyses to contain IgA. The modes of kinetic neutralization of poliovirus type 2 with serum IgG (Fr. I), secretory IgA from whey (Fr. II-2) and stool extract (Fr. II) were very much similar. However, stool Fr. I showed pronounced deviation from linearity. It was confirmed by serological analysis that this fraction was composed of degraded products of the IgA molecule, Fab or the like. In conclusion, the mode of neutralization of poliovirus type 2 was not different between serum IgG and secretory IgA derived from whey and stool extract.
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