DIGESTIBILITY OF SOY-BEAN AND PEANUT FLOURS. "q 
the nature and nutritive value of proteins, especial attention being 
given to the amino acids supplied. While it was found that under 
some conditions tyrosine, cystine, arginine, histidine, glutamic and 
aspartic acids may act as limiting factors in the diet, it seems to be 
very generally recognized by these students of nutrition that the two 
amino acids, lysine and tryptophane, are of especial importance in 
the dietary, lysine being essential for ‘‘growth” and tryptophane 
essential for ‘‘maintenance.’’ In view of these conclusions it ap- 
pears desirable to compare the amino acids resulting from the hydroly- 
sis of soy-bean and peanut proteins with those obtained by the hy- 
drolysis of the common cereal proteins. The amounts of amino acids 
resulting from the hydrolysis of the principal proteins of some com- 
mon cereals are brought together in the following table for comparison 
with those obtained by hydrolyzing glycinin and arachin: 
Amino acids resulting from hydrolysis of proteins of cereals. 
Glycinin a Arachin,9 
ig : | Gliadin,| Zein,3 Rye,! Or yzinin,| Hordein,’ 
Amino acids. wheat.| corn. |prolamin.| rice. barley. |soybean.| peanut. 
Glycine cs RiAANS RL REI O rR 8 9 Pe eos 10.00 0. 00 0.13 5(?) 0. 00 0. 97 0.00 
PAULI ITI GA sss ae eee pee 12.00 9.79 1.33 53.7 43 hee ae 4.11 
ate 
Waline?: soe oa a a me eS 1 3.34 1.88 | Not iso- 5(?) 13 .68 1.13 
lated 
WAIECING Meets ee ee 16.62 19. 55 6. 30 514.3 5. 67 8.45 3.88 
IPTOMNO Rete rae oe one n eee oe 113.22 9. 04 9. 82 53:3 IBY Ti 3h Ui 1.37 
Phenylalanme..... .... - 22 =-3-.- 1 2. 35- 6. 55 2:40 1-5 2:0 5. 03 3. 86 2.60 
Aspartic acid ..... tas See 1,58 Lec 25 o 4 ne ee 3. 89 5.25 
ated. 
Glutamic activo ess ae en 1 43. 66 26.17 38. 05 514.5 43. 20 19. 46 16. 69 
Serine See one a ee ee 1.13 O25 06 (®) Not iso- | Not iso- | Not  iso- 
; lated lated lated. 
IS WROSINIGS srs =f o=e aa ae S 11,20 3.55 1.19 5.5 i 1. 67 1.86 5.50 
@yshineys3s225 eer ee ee Lordy ype Beye cie: tl Not esti- 61.26 | Not esti-|-2 22.22.22 1.85 
mated. mated. } 
IAT SININGS sat aso ess 22s = | 13.16 155 2.22 69.15 2.16 5. 12 13.51 
ERISHI GING: Seen aes ae et | 22.19 . 82 .39 6 3.32 1. 28 1.39 1.88 
mcinereetee eis Ek Ae pve dot 00 .00| 64.26 00 2.71 4.98 
IMI ON eC eee saan See ee 15,22 3. 64 5.11 6 3.23 4.87 2.56 2.03 
Tryptophane .....-..-.-----.---| 11.00 .00 | Present. ) Present. | Present. | Present. 
1 Jour. Biol. Chem., 9 (1911), No. 5, p. 426. 
2 Jour. Biol. Chem., 22 (1915), No. 2, p. 261. 
3 Amer. Jour. Sen ysiol, 26 (1910), No. 4, p. 304. 
4 Osborne, Ergeb. Physiol., 10 (1910), p. 86. (In the absence of a name for rye protein, Osborne Paterked 
to the alcohol soluble protein as rye prolamin.) 
5 Osborne, Ergeb. Physiol., 10 (1910), p. 112. 
6 Jour. Biol. Chem., 22 (1915), No. 2, p. 275. 
7 Osborne, Ergeb. Physiol., 10 (1910), p. 90 
8 Osborne, Ergeb. Physiol., 10 (1910), p. 132. 
9C.O. Johns and D. B. Jones. To be published in the Journal of OEE Chernigtey. 
It will be noted on referring to the above table that the earlier 
analyses of gliadin, zein, rye-prolamin, oryzinin, and hordein indi- 
cated that these proteins supplied little if any lysine and tryptophane. 
In the more recent studies of oryzinin and gliadin it was found that 
on hydrolysis these proteins yield appreciable amounts of lysine. An 
unpublished investigation by C. O. Johns and A. J. Finks, Bureau of 
Chemistry, shows that hordein on hydrolysis yields approximately the 
