124 EXPEEIMENT STATION RECORD. 



pinene and camphene, particularly l-camphene. Pinene was present in the 

 active and inactive form, but chiefly as 1-a-pineue, which yielded optically active 

 pinonic acid ( [a]p = about — 65° in chloroform) on oxidation. The presence of 

 /3-phellandrene and /3-pinene was also verified. In all the fractions which 

 boiled at 173° C, or over, 7-terpinene could be detected and yielded on oxida- 

 tion with alkaline permanganate a characteristic erythritol (melting point 

 237°), which corresponded in its properties to 1.2.4.5 tetrahydroxyhexahydrocy- 

 mene. The fraction of sesquiterpene also contained bisabolene found in the 

 essential oil of Bisabol myrrh and probably also cadlnene. 



Detection of saccharin in fatty, starchy, and protein-rich, foods, Tobtelli 

 and Piazza (Abs. in Chem. Ztg., 34 (1010), No. 10, p. 62i).— The foodstuff is 

 mixed with from 12 to 18 parts of sand and from 7 to 10 parts of slacked lime, 

 and, amid stirring, 50 cc. of concentrated alcohol. During this time the mix- 

 ture is heated on the water bath to the boiling point. From 5 to 15 cc. of a 

 saturated salt solution is then added, well mixed, and the fluid poured off. This 

 process is repeated from 3 to 4 times, the precipitate collected on the filter, and 

 washed with 40 cc. of hot alcohol, which also removes the extractive substances 

 and the fats. The alcoholic solution is then concentrated and extracted with 

 petroleum ether. The saccharin remains behind and the fats, etc., are re- 

 moved. To the salt of saccharin a slight excess of sulphuric acid is added and 

 the mass extracted with ether. 



The method is apparently also of value in the quantitative estimation of 

 saccharin. Various modifications of the method are made when other sub- 

 stances are examined. 



Identification of saccharin, Tortelli {Ahs. in Chem. Ztg.. 34 (1910), No. 70, 

 p. 621). — The saccharin obtained by the above method is reduced with mag- 

 nesium in a test tube. From the magnesium sulphid produced, hydrogen sul- 

 phid can be detected with the nitroprussid reaction. 



A new reaction for glucuronic acid, G. Goldschmiedt (Ztschr. Physiol. 

 Chem., 65 (1910), No. 5-6, pp. 389-303).— If to a trace of glucuronic acid or 

 glucuron, dissolved in 100 cc. of water, is added from 1 to 2 drops of a 15 per 

 cent alcoholic solution of a-naphthol, and then from 3 to 4 drops of concentrated 

 sulphuric acid, a green coloration having a bluish hue is obtained. If more 

 water is added the solution will have a violet color. 



Bapid detection of emulsin, E. F. Armstrong (Jour. Physiol., JfO (1910), 

 No. 3, p. XXXII). — A method which is based on the use of Guignard's sodium 

 picrate paper for the detection of the hydrogen cyanid produced. 



The caseification of raw milk by the rennets of boiled milk, C. Gebber 

 (Compt. Rend. Acad. Sci. [Parish, 150 (1910), No. 19, pp. 1202-1204).— In boil- 

 ing raw milk the lactoglobulin and lactalbumin are coagulated and become inert. 

 The author shows that a close relation exists between the presence of these 

 protein bodies and the resistance to coagulation by rennet. This explains why 

 boiled milk coagulates quicker than unboiled milk. 



Comparison between the mode of action of certain inhibitory salts and 

 proteins coag'ulated by heat on caseification by boiled milk rennet, C. Gerbeb 

 (Compt. Rend. Acad. Sci. [Paris], 150 (1910), No. 21, pp. 1357-1360).— The 

 inhibitory action of gold, copper, mercury, silver, and certain metals of the plat- 

 inum group does not exert itself upon the proteolytic diastase but upon the 

 casein, which it makes more resistant against the rennet contained in boiled 

 milk. These metals combine with the casein and do not act as antibodies but 

 as inhibitors. Lactoglobulin and lactalbumin, which are the resisting bodies 

 in raw milk against coagulation by rennet of boiled milk, also act on the casein 

 as inhibitors. Raw milk does not contain these substances in a free state but 

 in combination with the casein, with which it forms a complex. 



