282 EXPERIMENT STATION RECORD. [Vol. 41 



Anaphylaxis, allergy; antianaphylaxis, antiallergic therapy, R. Kraus 

 (Rev. Inst. Bad. [A7-gentina], 2 (1919), No. 1, pp. 1-18). — This is a summary 

 of modern investigations and theories regarding experimental anaphylaxis and 

 its chemical relationship to allergj\ 



Anaphylatoxin and anaphylaxis. — XI, ITltra-filtration and fractionation 

 of anaphylatoxin, P. H. DeIvruif and A. K. Eggekth (Jour. Infect. Diseases, 

 2.'f (1919), Ko. 6, pp. 505-532). — In continuation of the study of anaphylatoxin 

 and anaphylaxis previously noted (E. S. K., 37, p. 578), an attempt has been 

 made to locate the toxic principle of anaphylatoxin by applying various methods 

 of fractionation of serum i)roteins and by ultraliUrution. 



It was found that the toxic princii)le of rat and guinea pig anaphylatoxin 

 could be recovered on the globulin fractions of the serum. A'arious methods 

 of isolating these fractions were studied. The best results were obtained by 

 removal and purification of the serum proteins by precipitation of the serum 

 in the cold with absolute alcohol or acetone and extraction of the precipitate 

 with ether. In this process the toxic principle was recovered quantitatively on 

 the sei'um proteins, and by fractionation was concentrated on the euglobulin 

 fraction. 



By means of iiltra-tiltrntion, using a membrane prepared from a solution of 

 celloidin in alcohol-ether with castor oil and glycerin as modifying agents, 70 

 per cent of the total serum protein could be filtered off with a total retention of 

 the toxic principle in the sac. The results obtained are considered " important 

 in that they furnish an excellent and simple means of concentrating the toxic 

 principle, furnish material for a tentative hypothesis of the nature of the toxin, 

 and effectively exclude the notion that protein degradation products are con- 

 cerned in this toxicity." 



A preliminary report of the fractionation of primarily toxic normal and im- 

 mune sera is also given. Such toxins are not recovered on the euglobulin frac- 

 tion as in the case of anaphylatoxin Init on the wnter-soluble globidin. 



On the separation of antitoxin and its associated proteins from heat- 

 denatured sera, A. Homer (Biochcm. Jour., IS (1919), No. 1, pp. Jf5-55). — The 

 investigations on antitoxic sera previously noted (E. S. II., 40, p. 288) have 

 been extended to determine (1) "to what extent the limits for the pre- 

 cipitation with ammonium sulphate can be narrowed so as to include, in the 

 second fraction precipitates from heated sera, only those proteins with which 

 the antitoxin is definitely associated, and (2) whether or no the antitoxin is 

 evenly distributed throughout the protein fractions precipitated at successive 

 stages between the limits indicated in (1)." 



The results indicate that, for the complete recovery of antitoxin during the 

 concentration of sera showing a heat-denaturation of 35 per cent or less by 

 fractional methods employing the use of anunonium sulphate, it is advisable to 

 precipitate the second fraction between 30 and 45 per cent of saturation with 

 the stilpbate, as reduction of the upper limit results in incomplete precipita- 

 tion of pseudoglobulin and antitoxin and I'aising of the lower limit results In 

 the precipitation of antitoxin in a form not readily soluble in brine. 



In heated sera showing a denaturation of 35 per cent or less, the bulk of 

 the antitoxin is associated with the proteins precipitated between 36 and 45 

 per cent of saturation with anunonium sulphate. The further fractionntion of 

 the protein isolated between these limits " showed that the percentage of the 

 total antitoxin precipitated between progressively increasing percentnges of 

 .saturation with the sulphate is directly proportional to the percentage pre- 

 cipitation of protein at the respective stages. From these oI)servations it is 

 clear that, in order to isolate antitoxin, means other than the fractional pre- 

 cipitation of the serum proteins must be emi)loyed." 



