2l8 



REPORTS ON INVESTIGATIONS AND PROJECTS. 



sufficient amount for such quantitative estimations of their decomposition 

 products. 



The determinations of the mono-amino acids have been made for the most 

 part according to the methods recently proposed by E. Fischer (Zeitschrift 

 fiir physiologische Chemie, 1901, xxxiii, 151) and those of the bases essen- 

 tiall}' according to the methods given by Kossel and his associates (Kossel 

 and Kutscher, ibid., 1900, xxxi, 161 ; Kossel and Patten, ibid,, 1903, 

 XXXVIII, 39). The general plan of these analyses has been that followed 

 by Abderhalden {ibid., 1903, xxxvii, 484) in analyzing oxyhemoglobin. 



In carrying out this work care has been taken to make the identification 

 of the substances determined as complete as possible and to weigh only such 

 products as examination showed to be essentially pure, so that the figures 

 given in the following table are to be taken as minimal, except possibly 

 those for prolin, which may be slightly too high owing to the well-known 

 difficulty of separating a/loi the other amino-acids from its alcoholic solution. 



The results of these analyses are given in the following table : 



Glycocoll 



Alanine 



Amino valerianic acid. 



Leucine 



aProlin 



Phenyl alanine 



Aspartic acid 



Glutaminic acid 



Serine 



Tyrosine 



Cystine 



Oxyprolin 



L5'sine 



Histidine 



Arginine 



Ammonia 



Tryptophane 



Total 



Gliadin. Glutenin. I,eucosin. 



Per cent. 



2.00 



.21 



5.61 



7.06 



2.35 



•58 



37-33 



•13 



1.20 



.45 



o 



.61 

 3.16 



Present. 



65.81 



Per cent. 

 0.88 

 4.64 

 .24 



5-95 

 4-23 

 1.97 



•91 

 23.42 



•74 



4.25 



.02 



1.92 

 1.76 

 4.72 

 4.01 

 Present. 



59-66 



Per cent. 



0-73 



4-45 



.18 



11-34 

 3-i8 

 3-83 

 3-35 

 6.73 



3-34 



2.75 

 2.83 



5.94 

 1.41 

 Present. 



50.06 



The analyses show that these three proteins are distinguished from one 

 another by differences so great that there can be no question that decided 

 differences in structure exist between them. Thus gliadin differs from 

 glutenin and leucosin by yielding no glycocoll and lysine and much more 

 prolin and glutaminic acid. Gliadin and glutenin each yield very much 

 more glutaminic acid and ammonia than leucosin, and less leucine. In 

 respect to the amount of these amino-acids, leucosin more nearly resembles 

 the animal proteins than the seed proteins thus far examined, and in this 

 connection it is interesting to note that leucosin occurs chiefly if not wholly 



