CHEMISTRY. 



521 



of the base to 1 of protein. This sohition after a tiine l)ecomes turbid, depositing 

 some of the dissolved protein. Edestin is sohible in a smaller amount of sodium 

 hydrate than of sodium carbonate. It conforms strictly with the definition of a 

 globulin, l^eing insoluble in water, but readily soluble in neutral solution (if sodium 

 chlorid of sufficient strength. Edestin mono-chlorid is insoluble in water l)ut solu- 

 ble in saline solutions, while i)otassium and sodium edestin are soluble in water and 

 insoluble in dilute solution of neutral salt, though solu])le in more concentrated solu- 

 tions. As edestin and its acid salts are soluble in neutral solution of sodium chlorid, 

 it shows that the solution of gloljulin does not depend upon an alkali, as stated 

 recently by Starke. 



A type of reaction by which sodium carbonate and hydrochloric acid, 

 may be formed in the animal organism, T. B. Osborne {Connecticut State Sta. Rpt. 

 1900, 2)t. 4, ()p. 441, 44~)- — From the examination of the resulting precipitate pro- 

 duced by carV)onic acid in a dilute sodium I'lilorid solution of edestin, the author 

 deems it probable that sodium carbonate and hydrochloric acid may be formed from 

 sodium chlorid in the organism. 



Sulphur in protein bodies, T. B. Osborne {Connecticut State Sta. lipt. 1900, pt. 4, 

 jjp. 443-471). — The author sought to determine as accurately as possible the total 

 sulphur in a considerable number of different proteids in order to learn if this element 

 forms a definite constituent of these substances, and also whether the fraction of this 

 sulphur converted into sulphid by heating with strong alkalis corresponds to a defi- 

 nite number of the atoms in the formulas calculated. Schulz's method of boiling in 

 a reflex condenser and recovering the sulphur as lead sulphid was followed in obtain- 

 ing the loosely-bound sulphur. These results were compared with those oljtained by 

 treating the proceids under pressure with strong alkalis at various temperatures. The 

 total sulphur was also determined, the method followed being described. The various 

 protein bodies from different sources were analyzed, the results being shown in the 

 following table: 



Sulphur content of protein bodies. 



Total 

 sulphur. 



Loosely- 

 bound 

 sulphur. 



Edestin 



Excelsin 



Legumin 



Vignin 



Amandin 



Glj'cinin 



Gliadin 



Hordein 



Zein 



Oxyhemoglobin from dog's blood 



Ovalbumin 



Ovovitellin 



Casein of cow's milk 



Per cent. 



0.884 



1.088 



.385 



.426 



.429 



.710 



1.027 



.847 



.60 



.5618 



1.616 



1.028 



Per cent. 

 0.346 

 .350 

 .166 

 .214 

 .217 

 .320 

 .619 

 .348 

 .212 

 .335 

 .491 

 .362 

 .101 



From an examination of the figures, of which the above represents averages, it 

 appears that those proteids which can be obtained in crystals, and therefore quite 

 pure, show a uniform proj)ortion of sulphur, and there can be no doubt but that 

 this element is a definite constituent of their molecules. The substanc-es, vicilin, 

 phaseolin, and conglutin gave no constant i)roportion of sulphur, and average figures 

 are not therefore reported. By using the simplest empirical formulas for a number 

 of proteids the molecular weights are calculated. These are regarded as only ajjproxi- 

 mate, since the methods of analysis precludes great accuracy. Carbon and nitrogen 

 may ])e determined with sufficient precision, but a slight error in sulphur leads to 

 serious differences in tlie formulas. A table is shown giving the composition and 

 formula ot a number of vegetable, animal, and compound proteids. 



