The Effects of Enzymes on Ragweed-Pollen and Studies on the Iso-Electric Point of Low-Ragweed Antigen

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Abstract
Summary and Conclusions: The acid-pepsin digestion of pollen-antigen does result in a definite loss in its activity. This loss is not due to digestion of the protein but to a decrease in the solubility of the pollen-antigen in the hydrochloric acid and to its oxidation. Such oxidation can be prevented by excluding oxygen during the process of digestion, or by the addition of dextrose. The iso-electric point of low-ragweed pollen-antigen, or of the protein which has absorbed large quantities of the active pollen-antigen, is pH 3.5. The preponderance of evidence as shown by this work and by the work of others indicates definitely that the enzymes of the gastro-intestinal tract destroy little, if any, of the pollenantigen. One can therefore reasonably conclude that, as far as its resistance to digestion is concerned, pollen-antigen is well adapted for oral therapy. This is particularly true if dextrose is given with the pollen.

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