222 



EXPERIMENT STATION RECORD. 



The wide range in the percentages of basic nitrogen in the different proteins is con- 

 sidered the most striking feature shown by these figures. The ammonia also showed 

 marked variations. 



Cotton-seed meal and gluten meal examined by the same method showed marked 

 differences in the ])ercentages of nitrogen in the different groups, but the authors sug- 

 gest that these chemical differences are a])]iarently of but little im])ortance from the 

 standpoint of animal imtrition. 



The precipitation limits with ammonium sulphate of some vegetable 

 proteins, T. B. Oshorxe and I. F. IIakkis {Join-. Arner. Cliem. Soc, 25 {1903), No. 

 8, pp. 837-842). — In the determinati<jns reported a quantity of protein was dissolved 

 in one-tenth saturated ammonium sulphate solution, the solution filtered, and 2 cc. 

 mixed with enough one-tenth saturated sulphate solution so that when precipitated 

 with a saturated sulphate solution the final volume would be 10 cc. In the folhiwing 

 table are given the cubic centimeters of saturati'd sulphate solution required to first 

 render the solution permanently turbid, to precipitate the bulk of the protein, and 

 to remove all traces of the substance: 



Saturated ammonium sulphate solution required to precipitate vegetable jjroteins. 



Name and source of protein. 



Globulin (English walnut) 



Globulin (black walnut) 



Edfstin (hemp seed) 



Edestin monochlorid 



Globulin (flaxseed) 



Globulin ( castor bean) 



Globulin (squash seed) 



Amanditi (almond) 



Corylin ( till icrt ) 



Excclsin (Brazil nut) 



Conglutiu — less soluble portion (lupine).. 

 Conglutin— more .soluble portion (lupine) 



Globulin (cotton seed) 



Legumin (vetch, lentil, horse bean) 



Phaseolin (kidney bean) 



The specific rotation of some vegetable proteins, T. B. Osborne and I. F. 

 Harris {Jour. Amer. Chem. Soc, 25 {1903), No. 8, p>P- 842-848) .—The averages of 

 numerous determinations, calculated to degrees of circular polarization, are as fol- 

 lows: Edestin (hemp seed) —41.3, globuhn (flaxseed) —43.53, globulin (squash 

 seed) —38.73, excelsin (Brazil nut) —42.94, amandin (almonds) —56.44, corylin 

 (filbert) —43.09, globulin (English walnut) —45.21, globulin (black walnut) -44.43, 

 phaseolin (kidney bean) —41.46, legumin (horse bean) —44.09, zein (corn) —28.00, 

 ghadin (wheat) —92.28. 



The globulin of the English walnut, the American black walnut, and the 

 butternut, T. B. Osborne and I. F. Harris {Jour. Amer. Chem. S<»:, 25 {1903), 

 No. 8, pp. 848-853). — A study of protein preparations from the nuts of Juglans regia, 

 J. nigra, and J. cinerea showed a close agreement as regards the percentages of nitro- 

 gen in the different decomposition i)roducts and the specific rotation. The globulins 

 from the different sources are therefore considered identical, and the name juglansin 

 is given them. In comparison with the globulin (corylin) from the filbert the only 

 positive difference was in the greater quantity of ammonia (about 0.4 per cent) 

 yielded by corylin, which has led the authors to conclude that the globulins of 

 Juglans and Corylus are chemically distinct. 



The carbohydrate group in the protein molecule, T. B. Osborne and I. F. 

 H.\RRiK {Jour. Amer. Cliem. Soc, 25 {1903), No. 5, jip. 474-478) .—The Moliseh reac- 

 tion was not ol)tained with avenalin, edestin, and globulin, and the reaction with a 

 large number of other vegetable proteins was so sliglit as to be attributed to a con- 



