STUDIES ON PHOTO-OXIDATION OF ANTIGEN AND ANTIBODIES

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Abstract
Serological, chem. and electrophoretic studies of photo-oxidised egg albumin, anti-egg albumin rabbit serum and anti-pneumococcus Type I horse serum were made. Photo-oxidation was produced by exposing the various substrates to visible light in presence of hematoporphyrin or eosin. Quantitative pre-cipitin estimations showed that progressive photo-oxidation progressively destroyed the antigenic function of egg albumin and caused a progressive lowering of the potency of the antisera; the specific antibody fractions behaved similar to the antibodies in whole sera. Egg albumin whose precipitin reaction had been destroyed by photo-oxidation no longer caused anaphylaxis in guinea-pigs and did not produce precipitins in rabbits. Chemical studies of progressively photo-oxidized egg albumin showed a progressive destruction of tryptophane and histidine, while tyrosin remained intact and cystine was reversibly oxidized. Similar studies of the globulin [gamma] fraction of anti-egg albumin rabbit serum and of Felton soln. of antipneumococcus serum showed no diminution of these amino acids in photo-oxidized material whose antigenic properties had been destroyed. The non-coagulable N and the amino-N of egg albumin, antisera or their specific antibody fractions showed but an insignificant increase during photo-oxidation, indicating that the loss of the precipitin reaction was not due to splitting of the respective protein molecules. Electrophoretic studies of these materials showed that photo-oxidation caused a marked alteration of the pattern of these substrates. Aggregates were formed indicating denaturation. The sensitiizers migrated with the albumin fraction of the unaltered as well as the photo-oxidized sera. In isolated proteins such as egg albumin, globulin [gamma] or Felton soln. the dye migrated independently of the protein. After photo-oxidation both the hematoporphyrin and the eosin became progressively fixed to the protein and migrated with the boundary.

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