T. B. Osborne and A. J. Wakeman 251 
to 20°. On adding water to this transparent deposit it becomes 
opaque and fails to dissolve. Possibly this less soluble frac- 
tion is an acid compound which differs from the more soluble 
part in the kind or quantity of combined acid. The solution in 
aleohol of 50 per cent by volume remains clear on adding alcohol 
to 70 per cent at about 20°. The solubility in alcohol of various 
degrees of concentration depends much on the temperature. 
Below 30° the solubility rapidly diminishes. When suspended in 
water containing a very little acetic acid the alcohol-soluble 
milk protein dissolves completely. This solution becomes opales- 
cent when heated to about 45° and at 80° is milk-white, but 
no flocculent coagulum separates on boiling. When an equal 
volume of absolute alcohol is then added a water-clear solution 
results at once. When this clear solution is poured into water 
an abundant separation occurs. If, instead of alcohol, sodium 
chloride is added, no visible separation of particles takes place, 
but, on standing, the solution separates into strata of differing 
opacity and an oily deposit slowly forms which is readily soluble 
in relatively strong alcohol. 
Dissolved in very dilute acetic acid this protein yields a volu- 
minous precipitate on adding potassium ferrocyanide. 
It gives strong tryptophane, Millon’s, and biuret reactions. 
From the behavior of this protein towards water, and its 
reaction with potassium ferrocyanide it is evident. that it is not 
to be considered as belonging to any group of the proteoses. 
Its preeminent solubility in relatively strong alcoholic solutions 
distinguishes it from any type of protein heretofore discovered 
in animal tissues or products. The possible existence of pro- 
teins of similar solubility ought to be considered whenever the 
complete removal of protein is necessary for the isolation of 
non-protein nitrogenous substances of animal origin. 
