428 
R. P. WODEHOUSE 
Summary 
The five proteins globulin, gliadin, glutenin, leucosin and natural 
proteose were prepared from wheat according to the method of T. B. 
Osborne, and when they were compared in their anaphylactogenic 
properties with each other, with an artificial proteose prepared by 
hydrolysis from glutenin, with the whole wheat preparations and with 
the proteins of other cereals, it was found that (i) all are anaphylacto- 
genic, but no two are immunologically exactly alike, (2) the natural 
proteose is the most active, (3) the natural proteose is different from 
the artificial proteose, (4) in any given case where whole wheat gives a 
reaction and in some where it does not some one or more of the in- 
dividual proteins are sure to be found to be more active, (5) it does 
not necessarily follow that because a case is allergic to wheat it will 
be found to be also hypersensitive to the other cereals (though this is 
sometimes the case especially if sensitization is of a high order), (6) it 
probably does not follow that sensitization to the seed proteins of 
cereals necessitates sensitization to the pollens of the same species, 
though not enough experiments were done upon this to more than 
suggest that it is a problem that ought to be further investigated. 
It is also shown that heating, except to very high temperatures, 
does not materially affect the anaphylactogenic properties of the wheat 
proteins. 
Medical Clinic of the 
Peter Brigham Hospital, 
Boston, Mass. 
LITERATURE CITED 
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Nuttall, G. H. F. The New Biological Test for Blood in Relation to Zoological 
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Osborne, T. B. Die Pflanzen Proteine. Ergebn. Physiol. 10: 47. 1910. 
Darstellung der Proteine der Pflanzenwelt. Abderhalden, Handb. Biochem. 
Arbeitsmeth. Berlin. 1910. 
Proteins of the Wheat Kernel. Carnegie Inst. Publ. 84. 1907. 
Osborne, T. B. and Clapp. Chemistry of the Protein Bodies of the Wheat Kernel III 
Hydrolysis. Amer. Journ. Physiol. 17: 231. 1906. 
Osborne, T. B. and Campbell. The Nuclei Acid of the Wheat Embryo and its 
Proteid Compounds. Journ. Amer. Chem. Soc. 22: 379. 1900. 
