68 Report of Schimmel § Co. 1921. 



Is there any more convincing proof for justifying our giving up the galenical 

 principle which, it is true, does not require much trouble, nor ingenuity, and for our 

 having recourse to the more conservative physical and biological methods, which will 

 lead to the aim desired by laborious and extensive studies, if carried out with the 

 necessary knowledge of the facts? 



Which then are the successes aimed at? 



In the first instance, it is possible to prepare a poison which, in its efficiency, exceeds 

 the simple extracts and poisons so far known more than a hundred times without in 

 the least impairing its specific character. Secondly, the living organism responds to the 

 incorporation of the poison by so much increased counter-effects that we no longer find 

 thirty to forty antitoxin units per serum unit, as before, but three hundred and more. 



Are the methods of physical chemistry and applied biology used really conservative? 



The answer will be easy to anybody who understands such methods, and who has 

 thoroughly studied the paper, I have spoken of, on "Further Studies concerning Pollen 

 Toxin". Contrary to the views of Heyl and Hopkins, I state there expressly that, 

 so far, such methods had mainly been employed, for the preparation of antigens, as 

 were customary in chemistry and cognate sciences, that these methods could only 

 lead to entirely-incomplete explications owing to the instability of the material worked 

 with, and that the more refined biological methods should replace the chemical methods 

 of separation which fail in these cases. 



My researches are based upon biological methods and upon physical modes of 

 working. 



If now Heyl and Hopkins find a contradiction in my statements by pointing, on 

 the one hand, to a non-deterioration of the hay-fever poison by the pollen proteases, 

 on the other hand, to a complete destruction of the poison by an artifical protease, 

 the trypsin, this only shows that the fermentative methods and their effects are not 

 sufficiently at their command, if they create such contrasts. 



There are a series of proteases with tryptic effects which all differ as to their 

 specific power of attacking substrates, their effective temperatures and their efficiency. 

 The one ferment attacks only a certain protein, leaving others uninfluenced; another 

 ferment has its temperature optimum at 37° C. and becomes more or less inactive at other 

 temperatures; a third destroys the bricks of albuminoids to a certain extent, and so on. 



The trypsin proper now has the strongest known tryptic effect. It develops its 

 optimum force at blood temperature, and in alkaline solution. We cannot be surprised, 

 therefore, that it should in alkaline solution at a temperature of 37° C, given sufficient 

 time of action, also attack the components of the pollen toxalbumin causing the hay- 

 fever. Heyl and Hopkins, however, are again in error when they quote from my paper 

 on "the Investigation of Rye Pollen and of the Hay-Fever Poison in it" (Beitrdge zur 

 them. Physiol, u. Pathologie, vol. V, N°. 7 and 8) a remark to the effect that the treatment 

 with trypsin would lead to a loss of efficiency. The final paragraph 4 of my paper states 

 expressly that enzymes like pepsin and trypsin can not completely destroy the poison. 



Even if, however, a complete destruction by trypsin were possible, this action 

 cannot be compared at all to the fermentative influences of the pollen proteases. 

 The latter, it is true, must be counted among the tryptic ferments, but they do not 

 possess anything like the hydrolysing power of the trypsin and develop these weaker 

 effects only in alkaline solution and at the optimum temperature of 30 to 40° C. 



My direction as to the preparation of the intense pollen-toxin, on the contrary, 

 deals with the action of single pollen proteases upon the pollen albuminoids in neutra 

 media and in an ice-box at a temperature of 4 to 6° C. Its only purpose is to separate 



