Abstract
The effect of a wide variety of hydrolytic conditions on the immunological activity of rabbit antiovalbumin was examined. Papain-HCN hydrolysis produces a quarter molecule unable to flocculate with the antigen, but able to inhibit flocculation of the complete system. This inhibitory fragment appeared to have arisen from the terminal quarter of the molecule. Attempts to reduce the size of the inhibitor further without destroying its activity were only partially successful. A study of the interactions of antibody, inhibitor and antigen showed that complete inhibition of flocculation could be produced. Inhibition or flocculation could be reversed,and the conclusion was reached that inhibitor was probably competing with antibody for the same combining centers of the antigen. There was no evidence to suggest that the inhibitor was carried down by the specific precipitate when flocculation occurred in its presence.

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