THE DECOMPOSITION PRODUCTS OF PROTEIDS. n 
substance produced by the latter method, which Bhould yield carbonic 
anhydride on treatment with an alkali. As he considered it probable 
that this substance might be basic, he endeavoured to isolate it as a 
precipitate by means of phosphotungstie acid, a reagent which is of 
great value as a precipitant of basic or alkaloidal bodies. B) r this means 
he succeeded in isolating not one but two bases, which he named hjdne 
and lysatinine. 
Lysine has the formula < ' i: Il n X.,0.,. and is homologous with Jaffe's 1 
ornithin (CfiHjjNjO^ probably diamidovalerianic acid). Lysine is pro- 
bably diamidocaproic acid, (hi heating it to 120°-130° with barium 
hydrate, barium carbonate is formed. It will therefore account for some 
of Schiitzenberger's carbonic anhydride. 
Lysatine or lysatinine, the second base, is even more interesting. 
Its formula is either C', ; H 1; ,X.0 2 or C c H u X.,0, and is a homologue of 
either creatine (C 4 H a X T 3 0.,) or creatinine (C 4 H 7 N 3 0), according as the first 
or second formula is taken. 
It can be obtained pure as a double salt of its nitrate with silver 
nitrate, and this when boiled with barium hydrate for twenty-five 
minutes yields urea ; this is a decomposition exactly analogous to that of 
creatinine under the same circumstances. From 10 grms. of the 
double salt Drechsel obtained about 1 grin, of urea ; which is a large 
quantity when one considers that under the conditions urea is quickly 
broken up into ammonia and carbonic anhydride. 
This is the first time that urea has been obtained from proteid in laboratory 
experiments. Many years ago, Bechamp - stated that he had obtained urea 
from egg-white by the oxidising action of potassium permanganate. Lossen 3 
found that the substance Bechamp took for urea was guanidine, which 
probably came from small quantities of xanthine, present in the egg-white as 
an impurity, or, as Drechsel 4 points out, from lysatinine. Drechsel's method, 
it is important to notice, is one of hydration ; not, like Bechamp's, one of 
oxidation. 5 
It should be added that Drechsel's work was carried out in the first 
instance with casein, but his pupils have discovered lysine and lysatinine 
among the cleavage products of other proteids and proteid-like substances, 6 
and further that the same substances are formed dining pancreatic digestion. 7 
Hedin 8 has more recently arrived at the conclusion that lysatinine is not 
a chemical individual, but a mixture of lysine with another base called 
arginine. Arginine (C H 14 X 4 O,) was originally separated from vegetable 
tissues by Schulze and Steiger, 9 and subsequently it was found by Hedin 10 
1 Ber. d. deutsch. chern. Gesellsch., Berlin, Bd. x. S. 1925. 
2 Ann. d. Chern., Leipzig, 1856, Bd. 100, S. 247. 
3 Ibid., 1880, Bd. 201, S. 369. Between Bechamp's and Lossen's time the question was in- 
vestigated by Stadeler, Journ. f. prakt. Chern.. Leipzig, 1857, Bd. lxxii. S. 251 : Loew, ibid., 
1871, N.F., Bd. iii. S. 289 ; Tappeiner, ibid., 1871, Bd. civ. S. 408 ; and Bitter, Compt. 
rend. Acad. d. sc, Paris, tome lxxiii. p. 1219 ; all of whom except Patter failed to confirm 
Bechamp's results. 
4 Loc. cit. 
5 On the formation of urea by oxidation from many organic substances, see F. Hofmeister, 
Arch. f. exper. Path. u. Pharmakol., Leipzig, 1897, Bd. xxxvii. S. 426. 
6 Fischer (from gelatin), Inaug. Diss., Leipzig, 1890; Arch. f. And. v. Physiol., Leipzig, 
1891, S. 205. Siegfried (from conglutin), Ber. d. deutsch. chern. Gesellsch., Berlin, Bd. xxiv. 
S. 418 ; (from reticulin), " Ueber d. chern. Eigenschaften des retic. Gewebes," HaMlUation- 
schrift, Leipzig, 1892. Siegfried also obtained from conglutin a sweet substance 
(CgH, c No0 4 ), corresponding to one of Schiitzenberger's gluco-proteins. 
7 Hedin, loc. cit. 8 Ztschr. f. physiol. Chern., Strassburg, 1896, Bd. xxi. S. 297. 
9 Ibid., Bd. xi. S. 43 ; Ber. d. deiUsch. chern. Gesellsch., Berlin. Bd. xxiv. S. 2707 ; 1896, 
Bd. xxix. S. 352. 
lu Ztschr./. physiol. Chi m., Strassburg, Bd. xx. S. 186 ; xxi. S. 155 ; xxii. S.191. 
VOL. I. — 3 
