106 Dr.8.B.Schryver. Some Investigations Dealing [Aug. 12, 
solution investigated. This solution capacity was much less marked in the 
cases of caffeine (which acts only as a base in the presence of strong acids) 
and benzamide, and was entirely wanting in the case of the base para- 
toluidine. The solutions of salts of polybasic acids possessed, in the case of 
leucine and phenylalanine, a slightly higher dissolving capacity than did the 
salts of monobasic acids of corresponding surface tension and viscosity, and 
in this respect their behaviour was similar to that in the edestin system. 
Further investigation on this point is necessary, and also on the electrical 
charge carried by solid crystals. 
Minor differences in the solution capacity of salts of various metals were 
also noticed which could not be correlated with any physical property. Thus, 
for example, lithium salts possessed a slightly greater solvent capacity than 
did those of sodium and potassium (especially in the case of caffeine). 
Furthermore, strontium salts were intermediate in their action between those 
of calcium and barium, the calcium salts possessing a greater solvent 
capacity. These differences were often, however, only faintly marked. 
Summary and Conclusions. 
I. Complex substances which form colloidal solutions have the capacity of 
adsorbing other substances from those solutions, which, accumulating on their 
surface, interfere sterically with their chemical reactions. For this reason 
such colloidal substances do not in their reactions obey the ordinary laws of 
chemical mass action. 
II. This conclusion has been illustrated by a study of the action of formal- 
dehyde on Witte’s peptone. Pauli’s observations of the formation of protein 
salts of heavy metals can perhaps be explained in a similar way. 
III. The analogy between the action of salt solutions in inhibiting chemical 
reaction of the complex proteins, and of their capacity to dissolve globulins, 
was noticed; the greater the inhibitory action, the greater the solvent power. 
IV. These facts suggested an explanation of the chemical character of the 
globulins. These proteins are here regarded as substances of both markedly 
acid and markedly basic character, and capable of forming insoluble aggre- 
gates by the combination of the acid group of one molecule with the basic 
group of another; such aggregates will undergo a slight but definite 
hydrolysis in the presence of water, to form simpler dissociated globulin 
molecules. In the presence of salts, adsorption will take place on the surface 
of these simpler molecules, and thus prevent re-aggregation to the solid form 
and alter the hydrolysis equilibrium. The greater the adsorption of a salt, 
the greater, therefore, the solvent or disaggregating capacity of its solution 
for globulins. 
