Anti-A agglutinins from snail (Otala lactea) were studied for their
serological and immunochemical behavior. Column chromatography suggested
that the snail anti-A had a sedimentation constant of 4.3 with estimated molecular
weight of 42,000. These preparations were tested for Ouchterlony’s agar gel diffusion
and immunoelectrophoresis. The breakage of disulfide bonds with mercaptoethanol
affected the anti-A activity of the snail protein. Attempts were made to study
the percentage of anti-A active protein in these preparations and the amount of
anti-A protein required for agglutination of red cells.
The column chromatography of the partially purified lectin showed
two peaks and anti-A agglutinin was present in the first peak having 22.4 S, 15.4 S
and 6.9 S. Second peak having 4.2 S was nonspecific.
Further studies on the ‘specific’ preparation from column chromatography
showed that lectin was more specific for hog A than neopeptone A substance and
was not affected by mercaptoethanol treatment. Immunoelectrophoresis showed
variations in the A substance from hog and neopeptone.
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