204 EXPERIMENT STATION RECORD. [Vol.37 



A slight increase of the activity of inulase was noted in the presence of the 

 acids, while a great activation was afforded by the acid salts, especially 

 disodium citrate and monosodium phosphate. Alkaline salts, on the contrary, 

 appeared to exert a harmful effect on the activity of the enzym. 



Studies of arginase and urease in plants, A. Kizel (Kiesel) (Izv. Imp. 

 Akad. Nauk (Bui. Acad. Imp. Sd. Petrograd), 6. ser., 1915, No. IS, pp. 1331- 

 1364). — Confirming earlier findings the author ascertained the presence of 

 arginase and urease in Aspergillus niger, and also established the occurrence of 

 the enzyms in ergot on Secale comutum, in vetch {Vicia saliva), and in ripe 

 fruits of Angelica sUvestris, as well as the presence of urease in etiolated 

 sprouts of the white lupine. In previous work the existence of arginase in the 

 sprouts of the white lupine and both arginase and urease in meadow mush- 

 rooms had been established. 



The enzyms of A. niger were found not to split guanldin tetramethylenamin, 

 although there was a partial cleavage of tetramethylendiguanidin with the 

 formation of guanidin tetramethylenamin. The enzyms found in ergot, meadow 

 mushrooms, and vetch do not decompose either of these reagents. In the work 

 with the enzyms of the ergot, guanidin also remained unchanged. In some 

 experiments with the white lupine and red clover {Trifolium pratense), in 

 which only tetramethylendiguanidin was used, no cleavage of the reagent was 

 observed. 



The experimental procedures used and the data obtained are described in 

 detail. 



Effect of medium on proteolytic enzyms of plants. V. I. Palladin (/rr. Imp. 

 Akad. Nauk (Hiil. Acad. Imp. SH. Petrograd), 6. sir., 1916, No. 7, pp. 527-5SSi.— 

 Since proteolytic enzyms affect the activity of other enzyms, particularly the 

 oxidases, the author attempted to determine experimentally substances which 

 would check the action of the proteolytic enzyms but would not at the same 

 time be harmful to the oxidative enzyms. Treparations of yea.st and wheat 

 sprouts served as experimental material, and sucrose, glycerin, ethylenglycol, 

 pyroracemic acid, formalin, and sodium chlorid were testeil as inhibitors. 



Corroborative evidence was obtained in regard to the poisonous action of 

 formalin on the proteolytic enzyms of yeast. A 1 per cent solution of pyro- 

 racemic acid neutralized by pota.ssium hydroxid exerted practically no infiu- 

 ence. ThQ other substances were found to divide themselves into two groups, 

 electrolytes and nonelectrolytes. Nonelectrolytes retarded the action of proteo- 

 lytic enzyms in a manner proportionate to their concentration, while weak 

 solutions of the electrolytes stimulated the action of proteolytic enzyms. A 

 strong solution of sodium chlorid slightly inhibited the action, but in a nmch 

 less degree than any of the nonelectrolytes. 



It is concluded that the introduction of the harmless nonelectrolytes which 

 arrest the action of proteolytic enzyms should have a beneficial effect on the 

 action of the enzyms in alcoholic fermentation. Notwithstanding the fact that 

 zymase may also be affected by nonelectrolytes. the formation of carbon tlioxid 

 is increased with the increase of concentration of these substances until an 

 optimum of concentration is reached. Beyond this the nonelectrolytes may 

 entirely inhibit the action of zymase. 



Some auxoamylases, E. W. Rockwood (Ahs. in Proc. Iowa Acad. Sci., 2S 

 {1916), pp. 37-39). — The author designates nitrogenous substances (particu- 

 larly those containing an NHj group) which stimulate the activity of amylases 

 as auxoamylases. In the work reported glycin, tyrosin, hippuric acid, an- 

 thranilic acid, and asparagin were found to be active, while sulphanilic acid and 

 acid amids like urea, acetamid, and propionamid were inactive. 



