58 
MR. J. R. GREEN ON THE CHANGES IN THE PROTEIDS 
I may summarise my results on germinating seeds as under :— 
1. There exists in the Lupin seed a proteolytic ferment, working in an acid 
medium, and capable of converting fibrin into peptone, leucin, and tyrosin. 
2. This ferment exists in the resting seed in the form of zymogen, and the latter 
very readily, by-jthe action of acids, is transformed into active ferment. 
3. Its action is much interfered with by presence of too much neutral salt, and it is 
quite destroyed by the action of alkalies. 
4. It works with extreme slowness. 
5. Its action is much like that of pancreatic juice, but more hemialbumose is 
formed by it than by the latter. 
6. It acts on the proteids in the plant in such a way as to convert them into 
peptone, and then into leucin, asparagin, &c. 
7. The nitrogenous plastic material travels to the growing points in the form of 
these amide bodies, and not in that of peptone. 
8. The conversion of cellulose in the date seed into plastic material is not carried 
out by an isolable ferment in the endosperm, but by the gradual breaking down of 
the latter, brought about by the epidermal cells of the cotyledon, which contain the 
ferment in small quantity. 
The proteolytic ferment of the Lupin has considerable importance from the slowness 
of its action, which seems as if it would afford facility for the examination in detail of 
the course of proteolysis. In the foregoing paper I have called attention to two 
points that seem to offer a field for further investigation. The first of these is con¬ 
nected with the apparent formation by this ferment of considerably more “ hemi¬ 
albumose ” from fibrin than is formed from it by either pepsin or trypsin. Whether 
hemialbumose be a single body, or more probably a mixture of several, it appears to 
approach the globulins in its reactions more nearly than does the acid-albumin or 
parapeptone, which is formed coincidently or later. Thus, like them, it is more freely 
soluble in dilute salt solutions than it is in water, in which fluid globulins are 
altogether insoluble. From its solution it is precipitated on saturation with the 
same neutral salt; at least part of it is precipitated by dialysis or dilution, just as 
most globulins are. In its behaviour to heat it beo-ins to show a difference. Both 
globulins and hemialbumose form opalescent solutions in the cold; on raising to a 
temperature above 70° C., the globulins are coagulated; the hemialbumose goes into 
solution completely, being again thrown down on cooling. This difference is carried 
a step further*with parapeptone, for when in solution it is quite unaffected by heating 
or cooling. There is, however, a difference between the latter two bodies as to the 
liquid in which they are soluble. In the peptones the solubility at all temperatures 
is still seen, and the necessity for acid or alkaline reaction in the fluid to secure such 
solubility has disappeared. The point suggested is, therefore, whether hemialbumose 
is really the first product formed, and whether it gives rise later to the other products 
seen, viz., parapeptone and peptone. If so, the greater quantity of it found with the 
