EXPERIMENT STATION RECORD. 



Vol. XXVI. Abstract Number. No. 3. 



RECENT WORK IN AGRICULTURAL SCIENCE. 



AGRICULTURAL CHEMISTRY— AGROTECHNY. 



A text-book of physiological chemistry, O. Hammarsten, trans, by J. A. 

 Mandel (Xcio York and London, 1911, 6. ed., enl. and rev., pp. VIII-^96.'i). — 

 This is the sixth English edition, and a translation from tlie seventh German 

 edition, which is greatly enlarged, thoroughly revised, and brought up to date. 

 A new chapter on physical chemistry is added, while the chapter on the ani- 

 mal cell has been incorporated in other chapters. 



A color reaction for proteins with sodium nitroprussid, V. Aenold (Ztschr. 

 Physiol. Chem., 10 (1911), Ko. J,-5, pp. 300-309; abs. in Zcnthl. Gesam. Physiol, 

 u. Path. Stoffivechsels, n. scr., 6 {1911), No. 10, p. 408).— The reaction is as 

 follows: To from 1 to 2 cc. of the solution containing the protein from 2 to 4 

 drops of a 4 to 5 per cent solution of sodium nitroprussid is added, and then 

 a few drops of ammonium hydroxid. If a protein is present a purple-red colora- 

 tion is obtained. Among the products of protein cleavage cystin alone gives 

 the reaction. 



Hydrolysis of the protein of linseed, F. \V. Foreman (Jour. Agr. Sci., 3 

 (1910), No. .',, pp. 358-3S2; ahs. in Intermit. Inst. Agr. [Rome], Bui. Bur. Agr. 

 Intel, and Plant Diseases, 2 (1911), No. 3, pp. 492-.'i9-'i).— The fohowing 

 figures were obtained by the author as a result of hydrolyzing the protein 

 contained in linseed meal : Glycin present, alanin 1.03 per cent, valin 12.71 per 

 cent, leucin and isoleucin 3.97 per cent, prolin 2.85 per cent, phenylalanin 4.14 

 per cent, aspartic acid 1.65 per cent, glutaminic acid 11.58 per cent, serin 

 present, tyrosin 0.65 per cent, arginin 6.06 per cent, histidin 1.66 per cent, lysin 

 1.19 per cent, ammonia 1.94 per cent, and tryptophan present. 



From these figures it may be noted that the valin fraction is very high, while 

 that of tyrosin is very low. 



The coagulating point of egg, serum, and milk albumin, and serum globu- 

 lin in ammonium sulphate solutions, K. Micko (Ztschr. Untersuch. Nahr. u. 

 Genussmtl., 21 (1911), No. 11, pp. 6-'t6-654, pi. 1; abs. in Ztschr. Angew. Chem., 

 2It (1911), No. 31, p. 1^91). — By determining the coagulating point of proteins 

 in 2 solutions of known but different degi'ees of saturation with ammonium 

 sulphate, the temperature at which turbidity sets in and the precipitation point 

 being noted, it is possible to identify the various proteins present in the solution. 



Constitution of vicianose and of vicianin, G. Bertrand and G. Weisweilleb 

 (Conipt. Rend. Acad. Sd. [Paris], 151 (1910), No. 20, pp. 88^-886; abs. in Jour. 

 Chem. Soc. [London], 100 (1911), No. 579, I, p. 15). — Vicianose was oxidized 



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