CHEMISTRY. 



517 



found to be impure, containing helianthotannic acid. Attempts were 

 then made to prepare globulins free from helianthotannic acid by 

 extracting- the meal with alcohol before precipitating the proteid, but 

 "it was found practically impossible to remove the acid so completely 

 as to obtain no yellow reaction when the extract was treated with 

 potash." The composition of 3 preparations was as follows: 



Composition of sunflower globulin. 



Preparation 



10. 



Carlwu . . . 

 Hydrogen 

 .\ itrogen 

 Sulphur . . 

 Oxygen .. 



Ash 



Per cent. 



.".1.27 

 0. 55 

 18.21 

 .78 

 23.25 



100.00 

 .31 



Preparation Preparation 



12. 13. 



Per cent. 



51.58 



c, 55 



18.29 



.97 



22.61 



Per cent. 



51.54 

 6. 99 



18.58 



1.00 



21.71 



100. 00 



100.00 

 .47 



Preparation 13 was the purest and was very nearly white in color. 

 The characteristics and reactions of the globulin are described: 



"In composition and reaction this preparation agrees with the globulin edestin 

 except that a part is precipitated by saturating its solutions in brine with sodium 

 chlorid. In composition the part precipitated by saturating with salt and that 

 remaining in solution an- alike. . . . 



'• As helianthotannic acid contains about '>'■'< per eeut of carbon, the presence of 2 

 per cent of this acid in our preparation would but slightly raise tin- figures obtained 

 for carbon and reduce those fornitrogen by about 0.35 percent. The composition of 

 the purer preparations which we have obtained differ from edestin to about this 

 extent. 



"It is therefore our opinion that the sunflower seed contains as its principal pro- 

 teid the globulin edestin, but that as obtained by extraction from the seed, this is 

 mixed with helianthotannic acid, from which we have not succeeded in separating 

 it completely."' 



Tines states that if the aleurone grains of sunflower seed are treated 

 with alcohol the globulin of which these grains consist behaves like 

 vitellin, i. e., dissolves in a saturated solution of sodium chlorid; but 

 the authors were unable to contirin these observations. 



Proteids of the cowpea, T. B. Oseorxe and G-. F. Campbell 

 (Connecticut State Sta. Rpt. 1896, pp. 380-380).— -The material examined 

 was prepared by coarsely grinding the peas, separating the black seed 

 coats by winnowing, and then grinding the coarse meal to a fine flour. 

 The method of treatment by which 13 preparations were made and the 

 composition and characteristics of these preparations are given in 

 detail. The authors summarize the results of their investigation as 

 follows : 



"(1) The ehief proteid of the eowpea is a globulin, much resembling the legnmin 

 of the pea and vetch, but essentially different in composition and properties, for 



