308 THE HEXONE BASES OF EGG-WHITE, 



dipeptide of Levene «fe Beatty.* Owing to this admixture the 

 lysin nitrogen was calculated from the lysin picrate as 0*054 gm., 

 and not from the nitrogen precipitated by the phosphotungstic 

 acid, viz., 0-147 gm. 



On the other hand, 17-36 % in the second hydrolysis is a low 

 figure, since the method of Hausmann gives 21-33 %. Our low 

 figure is due to the incomplete washing of the precipitate of 

 barium sulphate and phosphotungstate. 



The figures of histiclin and arginin agree well. It must be 

 pointed out that a considerable loss of nitrogen occurred with 

 each precipitate of barium sulphate, with the result that the 

 nitrogen figures do not add up. Thus, in experiment ii., 0*548 gm. 

 nitrogen as lysin plus 0-19 gm. other than lysin, or 0-74 gai. 

 nitrogen were obtained from 1-095 gm. nitrogen present originally. 



The protein in the second hydrolysis amounted to 89-6 gm. 

 The lysin calculated from the nitrogen present in the solution 

 from which the lysin picrate was precipitated was 2-86 gm. The 

 lysin picrate once recrystallized weighed 547 gm. 



0'133gm. lysin picrate gave 17'5 c.c. ^ NHg by Kjeldahl- 

 Jodlbauer-Gunning method. 



C6Hi4N202.CfiH2(N02)30H requires 18-66% N. Found 

 18-42% N. 



The solution of histidin contained nitrogen equal to 0-59 gm. 

 histidin. There was crystallized 0*25 gm. histidin dichloride ai.d 

 0-484 gm. picrolonate. 



0-0618 gm. histidin dichloride gave 0-0762 gm. AgCI. 



CeH9N3O2.2H01 requires 31-18 % 01. Found 30 5 % 01. 



It was noted that the histidin dichloride gave a slight residue 

 of barium salt upon combustion. 



The solution of arginin contained nitrogen equivalent to 

 2-14 gm. arginin. A portion was lost, but from a fraction con- 

 taining 0-433 gm. nitrogen, 2-437 gm. arginin nitrate were 

 obtained. The arginin nitrate was converted into arginin copper 

 nitrate. 



* Loc. cit. 



