Abstract
SummaryBALB/c histocompatibility antigen solubilized by Triton X-100, and a small molecular form derived from it by digestion with papain, were examined for inactivation by periodate and for carbohydrate content. Treatment with a low concentration of periodate reduced by about 75% the antigenic activity of the original macromolecular form of the antigen, as judged by inhibition of anti-BALB/c alloantibodies in several in vitro tests, but did not have this effect on the small molecular unit. Also, carbohydrate analysis of the macromolecular antigen showed it to contain mannose, glucose, glucuronic acid and n-acetyl galactosamine, whereas no sugars were detectable in the small molecule.
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