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In a comparative study of rabbit antiovalbumin and the inert y-globulin with which it is associated (Porter, 1950) no definite difference in structure was found to which the specific biological activity of the antibody could be attributed. The active and inactive material apparently exist as single long polypeptide chains of about 1500 amino-acid residues, the terminal tetrapeptide being, in each case, alanylleucyl-valyl-aspartyl-. There remain a great rnany possibilities of variation in structure, but the results already obtained suggest that considerable similarity may be found between normal y-globulin and antibody and that antibody may differ from normal yglobulin only in that segment of the chain which is responsible for combination.with antigen. The lattice theory of antibody, antigen combination (Marrack, 1938) postulated that at least two combining areas should be present on each molecule to enable flocculation to occur. If the antibody molecule could be split to give fragments containing one such combining area these fragments should be capable of combining with the antigen, but not of precipitating with it. They would therefore be expected to inhibit the flocculation of antibody and antigen by competing for the combining area of the antigen. As the combining centre of the antibody may be small enough to permit detailed chemical examination it seemedworth while to try to produce an inhibitor by hydrolysis of antibody. No such attempt to prepare an inhibitor from an antibody appears to have been reported, but Landsteiner (1942) studied the complementary problem of attempting to produce an inhibitor by hydrolysis ofan antigen. He was successful, but it is difficult to interpret his results. The antigen, which was degummed silk, was brought into solution by concentrated hydrochloric acid and after several precipitations was finally adsorbed on charcoal before injection. Degradation may have occurred during preparation and the nature of the material injected is uncertain. However, specific inhibition of the antisera could be effected by the addition of dialysable products from partially hydrolysed silk, and Landsteiner (1942) estimated the average mole-

The formation of a specific inhibitor by hydrolysis of rabbit antiovalbumin