O'Brien . — The Proteids of Wheat. 223 
Since writing the foregoing pages, my attention has been 
drawn by Prof. Green’s article in ‘Science Progress’ for 
March, 1895, to some work on the proteids of wheat (Amer. 
Chem. Journ., 1893 ; Journ. of the Amer. Chem. Soc., 1894) 
by Messrs. Osborne and Voorhees, with which I was unac- 
quainted. This work to some extent covers the same ground 
as my own, but our results are not altogether concordant. 
I find, however, that I am in agreement with these authors 
in my conclusions as to the ferment-theory of gluten-forma- 
tion, and as to the supposed origin of gluten from the globulin 
of flour. 
Apart from gluten, they find three proteids in flour which 
seem to correspond to those which I have described under 
somewhat different names, as indicated in the following table : 
Globulin [edestin] *6—7% ) 0 
Albumin [leucosin] \V*4% ) 
Proteose 
corresponding to Vitellin ) Globulin 
„ „ Myosin \ 1%. 
„ „ Proteose. 
Leucosin is described as an albumin with the exceptional 
characters (1) of being precipitated on saturation with ammo- 
nium or magnesium sulphates, and (2) of coagulating at the 
low temperature of 52°C. ; whereas the conclusion at which 
I have arrived is that this proteid is a globulin of the myosin- 
class. 
These authors describe the proteids of gluten as follows : 
Sol. in dilute alcohol . . . Gliadin 4%. 
„ only in dilute acids or alkalies . Glutenin 4%. 
They thus return to the view of Taddei, and in part to his 
terminology. Whilst they reject his term ‘ zymom,’ as 
implying ferment-action, they retain ‘ gliadin ’ for the sub- 
stance which I have termed £ glian ’ on account of the varying 
sense in which the term ‘ gliadin 5 has been used by different 
writers, having been applied sometimes to the whole, some- 
times to a part only, of the alcohol-soluble constituents of 
gluten. Moreover, the view which they adopt as to the 
mutual relation of these two substances differs essentially 
from that which my observations seem to suggest. They 
