276 
After 3 days: 
‘weigh Clotting Color Weight | Clotting |Colorim., Weight |Clotting| Colorim. 
with milk} I 2.24 | 2 min. | 3.0 Il 2.24 4 min. ol, an 2.20| 9 min. 0.5 
' , meas- 
without „ 2:20 as Bel II 2.40 |23/, hour cane III 2.30} none 0 
After 4 days: 
with milk! I 2.25 | 2 min. 1.4 IL 2.36 | 3 ‘min. 155 HI 2.40/20 min. 0.8 
not 
measurable 
without „ |1250| 2,» | 1:6 |1 2.50 | 1 hour! 0.4 |III 2.25| none 
| 
through adsorption it combines with the protein still in another 
manner in consequence of the chemical structure of the molecules. 
When this compound breaks down, in which process the action of 
the enzyme manifests itself, the liberated enzyme is supposed to 
attach itself to other still intact protein molecules which are lying 
on the periphery and to advance in this way in the direction of 
the diffusion-current. If this supposition is correct, the movement of 
the pepsin must also be promoted by albumoses, which it is still 
able to attack; not, however by animo-acid freed from the protein 
which pepsin cannot attack and which, in contradistinction to 
albumoses, it cannot grasp‘) in an electric field. 
To this end we mixed, in the manner described above, first, 
primary and secundary albumoses, prepared by digestion of fibrin 
with gastric juice, and then a mixture of pure amino-acids approxi- 
mately in the relation in which they are contained in fibrin, in a 
solution of 0.2°/, HCl, with the same volume of 3°/, agar-agar. 
The primary albumoses contained a considerable amount of hete- 
roalbumose, the secondary ones were freed as much as possible 
from primary ones by repeated half-saturation with ammonium- 
sulfate and by filtration. 
Primary albumoses. Two tubes each with 100 mgrs. of albumose, 
two without albumose, prepared as usual. 
It appears then that, while the primary albumoses largely promote 
the movement of the enzyme, the action of the secondary ones, 
which are much less attacked by pepsin, though it cannot be entirely 
denied, is much less significant. 
Nothing, however, could be detected of an action of the amino- 
acids, ‘as is shown by ithe following experiment: 
) Vide Rineer, Zeitschr. f. Physiol. Chem. XCV, 195 etc. Onderz. igs oe Laborat. * 
Utrecht. 5de R. XVI, 282. . . 
