4i8 
R. P. WODEHOUSE 
Leucosin is soluble in pure water or in water faintly acid or alkaline 
in reaction but is precipitated in an insoluble coagulum from a faintly 
acid solution by heat. 
Wheat Globulin. In neutral media this is soluble only in saline 
solutions, the one generally used being lo percent NaCl. 
Gliadin is soluble in 50-80 percent alcohol but insoluble in water 
or absolute alcohol. 
Glutenin is insoluble in w^ater, alcohol or neutral salt solution but 
readily soluble in weak alkali, 1/5 percent being generally used. 
Proteose is soluble in water and not precipitated by heat. 
All of the proteins soluble in water or salt solutions may be pre- 
cipitated by saturating their solutions with ammonium sulphate. 
Whether these proteins are chemical individuals or whether we 
have to seek further separations is not definitely known. None has 
been prepared, as yet, in a crystalline form. Though some vegetable 
proteins have been crystallized, wheat globulin which, of the wheat 
proteins, approaches nearest to this condition, occurs only in more or 
less regular spheroids. 
There is pretty good evidence to show that all of these proteins, 
including the '^natural proteose,'' exist preformed in the seed. Pro- 
teoses are generally regarded, however, as being the first product of 
hydrolysis of the higher proteins. Still Wells and Osborne (Wells 
and Osborne, '15) furnish good evidence that the "natural proteose'' 
is not a product of hydrolysis but is a naturally existing protein of the 
seed. 
The artificial proteose was prepared by hydrolysis from glutenin (as 
will be shown) and was used throughout the wheat experiments for 
comparison with the natural proteins in general and more especially 
to see if a proteose, known to be the product of hydrolysis, would give 
biological reactions similar to those of natural proteose. 
Besides these individual proteins there were used in this work two 
whole wheat" protein preparations made, one from raw wheat and 
the other from bread, by the author (Wodehouse, '16). Of course 
these two preparations do not, as their name might imply, contain 
all five of the wheat proteins in anything like equal proportions. On 
the contrary the solubilities, as indicated above, would prevent such 
preparations from containing more than a trace of glutenin and 
gliadin, and the bulk would be made up of the natural and decom- 
position proteoses together with leucosin and globulin where they were 
not precipitated by heat. 
