CHEMISTRY. 



515 



The composition of conglutin as obtained by us is shown by the following ligures : 



. Conglutin. 



Carbon... 

 Hydrogen 

 Nitrogea. 

 Snlphur.. 



Oxygen . . 



Yellow Bine 

 lupine. lupine. 



Per cent. 

 50.91 

 6.88 

 17.93 

 .52 

 23.76 



Per a', it. 

 51.13 

 6.86 

 18.11 

 .32 

 23.58 



100. 00 



100. 00 



"Conglutin is readily soluble in sodium chlorid solutions containing upward of 

 5 per cent of the salt. By sufficient dilution it is precipitated, :i sirnpy liquid sep- 

 arating which is rendered opaque and solid by treatment with water. Dissolved in 

 salt solution, it is apparently unaffected by prolonged heating in a boiling water 

 bath, but solutions thus heated on standing and cooling form a solid opalescent jelly, 

 which becomes clear and fluid on again heating. Unlike other globulins, conglutin 

 does not yield insoluble (coagulated) products by washing with alcohol or dryiug. 



"After exhausting lupine meal with salt solution a small quantity of proteid can 

 be extracted by 0.2 per cent potash water, from which it is precipitated by adding 

 acetic acid in slight excess, but not by making the solution neutral to litmus. Only 

 one preparation of this substance was made, which gave the following results on 

 analysis : 



Proteid soluble in potash water. 



Per (in i. 



Carbon 51.40 



Hydrogen (>. 79 



Nitrogen 16. 43 



Sulphur 1. 03 



Oxygen 24. 35 



100. 00 



"Owing to the insolubility of this substance in any but alkaline fluids and the 

 difficulty of making preparations of known purity nothing further was learned 

 respecting it." 



Effect of minute quantities of acid on the solubility of globu- 

 lin in salt solutions, T. B. Osborne and G. P. Campbell (Connecti- 

 cut State Sta. Rpt. 1896, pp. 369-373). — In investigations on the proteids 

 of the castor bean (E. S. R., 4, p. 934) it was found that the principal 

 globulin was partly soluble and partly insoluble in a saturated salt 

 solution, and that these 2 parts are alike in composition but slightly 

 different in reactions. Later a proteid was found in sunflower seed 

 (p. 51C) having similar composition and properties, which led the authors 

 to a further study of the globulin of the castor beau with a view to dis- 

 covering the cause of the partial insolubility in a saturated salt solution. 



Preparations were made of the fractions of the globulin soluble in 

 cold 10 per cent brine and not precipitated by saturation with salt (A) 

 and of those soluble in cold and hot 10 per cent brine, respectively (B 

 and C), but insoluble in saturated brine. Analysis showed that the 



