346 



SCIENCE 



[N. S. Vol. XXVI. No. 663 



for venom. On the other hand, pure serum 

 globulins or serum albumins are not venom 

 activating, notwithstanding their content of 

 alcohol-extractable lecithin. Non-activating 

 serum can be made activating by adding small 

 quantities of oleic acid or oleate soaps. 



The degrees of susceptibility of corpuscles 

 are parallel to the amounts of fatty acids 

 which they contain. The absence of fatty 

 acids is associated with total insusceptibility 

 of the corpuscles to the hemolytic agent of 

 venom. The amounts of lecithin extractable 

 from corpuscles are about the same in dif- 

 ferent bloods and bear absolutely no relation 

 to susceptibility. The addition of adequate 

 amounts of calcium chloride stops venom 

 hemolysis with washed corpuscles of suscep- 

 tible species. A previous addition of a small 

 amount of lecithin annuls protection by this 

 salt. A small amount of oleic acid or soluble 

 oleate soap, which is insufficient to produce 

 hemolysis alone, can render the corpuscles of 

 insusceptible species hemolyzable by venom. 

 An oily substance can be extracted with ether 

 from the stoma of susceptible corpuscles, but 

 not from the insusceptible varieties. This 

 oily mass is venom-activating, but contains 

 no lecithin. 



On the Influence of the Reaction, and of 

 Desiccation, upon Opsonins: Hideyo 



NOGUCHI. 



The author found that opsonins were most 

 active in neutral liquids. An alkalinity ex- 

 ceeding n/20 KOH prevented opsonization. 

 An acidity of n/SO HCl was sufficient to 

 stop the opsonic function of serum. Neutral- 

 ization of excessive alkalinity or acidity 

 caused reappearance of opsonic activity. On 

 the other hand, an alkalinity or an acidity 

 approaching that of the normal alkali or acid 

 produced a condition of irreversibility of the 

 inactivation. The opsonic index, estimated in 

 the normal alkaline reacting serum, was far 

 lower than that in a neutral medium. 



The high stability of opsonins against 

 desiccation and the high thermostability of 

 dried opsonins are very striking. Almost no 



reduction of opsonic strength is evidenced 

 after a serum is completely dried at 23° C. 

 within a few hours. In the dry state, opso- 

 nins are well preserved even after two years. 

 Temperatures below 150° 0. do not destroy 

 opsonins in the dry state. After heating at 

 150° C, dry serum becomes difficult to dis- 

 solve, but opsonins may still be detected in it. 

 Complements withstand desiccation and 

 dry heat in a manner similar to the resist- 

 ance of opsonins. 



On Becomposition of Uric Acid hy Animal 

 Tissues: P. A. Levene and W. A. Beatty. 

 In these experiments uric , acid was sub- 

 jected to the action of spleen pulp in the 

 presence of 2-per-cent. of ammonium hydroxide 

 and 2 per cent, of acetic acid. Under both 

 conditions 50 per cent, of the uric acid pre- 

 sent was decomposed. Allantoin was one of 

 the decomposition products. 



On the Diuretic Action of Thymin: P. A. 



Levene. 



The experiments were carried out on a dog 

 with an Eek fistula. The dog had been kept 

 on a purin free diet many weeks before the 

 experiment was begun. For three weeks 

 preceding the experiment the water consumed 

 by the dog and the urine eliminated were 

 carefully measured. It was noted that admin- 

 istration of thymin was followed by marked 

 diuresis. 



On Lysinglycyl attained in the Tryptic 

 Digestion of Egg Alumen: P. A. Levene 

 and W. A. Beatty. 



In the process devised by the vsriters a year 

 ago for preparing the peptid, prolinglycyl, a 

 substance was produced from egg albumen, 

 which, on further cleavage, yielded only lysin 

 and glyeocoU. The substance could not be 

 crystallized. The authors called attention to 

 the fact that peptids of the hexon bases ob- 

 tained by Fischer and Suzuki synthetically 

 also failed to crystallize. 



William J. Gies, 

 Secretary 



