102 Dr.S. B.Schryver. Some Investigations Dealing [Aug. 12, 
of the surface tension and concentration.* If, now, the rate of diffusion 
of the dissociated globulin molecules outwards from the limiting surface, and 
of the salt molecules inwards towards the same surface, be slow, the 
concentration of the globulin molecules at this point will be relatively high 
compared with that of the salt molecules, and a relatively small amount of 
adsorption will take place. As a consequence the dissociated molecules will 
tend to reageregate to form the solid globulin. The reverse will hold if 
diffusion be rapid. If the conditions be such that a large amount of 
adsorption takes place, the solid globulin will completely disaggregate and 
a diphasic system will be formed; on dilution the amount of salt adsorbed 
will be diminished and reagegregation will take place. 
From these considerations it will follow that the disaggregating action of salt 
solutions on the globulins is a function of two physical constants of the solutions, 
viz. the viscosities and the surface tensions. The higher the surface tensions and 
the viscosities, the smaller the disaggregatiny capacity. 
Quite similar considerations apply to the inhibitory action of salt solutions 
on the polymerisation or condensation of the methyleneimino-peptones. 
Here, again, three phases can co-exist, viz., the poly-product,f the simple 
methyleneimino-compound in colloidal solution, and the salt solution. If 
adsorption be sufficiently complete, the poly-product will not be formed, and 
the system will be diphasic. There is, however, a distinction between the 
system and the globulin system, which is probably more apparent than real. 
The precipitate formed by the addition of formaldehyde to Witte’s peptone 
becomes, after a very short interval, insoluble, 7c. it will not dissolve in those 
salt solutions which inhibit its formation; it is, however, soluble in such 
solutions immediately after it is formed. Possibly a further chemical action, 
such as dehydration or scission of formaldehyde, takes place after polymerisa-. 
tion, with the formation of a product which can no longer be depolymerised 
or re-converted into the simple methyleneimino-product by water. The 
formation of such a product will tend to alter the equilibrium. It may be 
recalled that serum globulin also becomes insoluble in salt solutions after 
standing under water for some time, and possibly also undergoes a secondary 
chemical change of similar nature. 
These conclusions have been confirmed by the quantitative investigation of 
the action of a series of salts on both the systems discussed above. The 
inorganic sodium salts—chloride, bromide and nitrate, iodide and sulpho- 
cyanide, mentioned in the order of decreasing surface tension—have a 
gradually increasing capacity for disaggregating globulins. Similar results 
* See adsorption equation given above. 
t This term is used to indicate the more complex product. 
