Globulins are a class of proteids which occur in both animal and vegetable tissues. They are peculiar in the complexity of their relations to electrolytes. Insoluble in water, they are soluble in low concentrations of acids, alkalies, or neutral salts. In presence of acids the globulin is electro-positive, in presence of alkalies it is electro-negative, in presence of neutral salts it is electrically neutral. Electrically active globulin ( i. e ., dissolved by acids or alkalies) is precipitated by minute amounts of neutral salts; also, no matter what its electrical state may be, or how dissolved, globulins are precipitated by neutral salts near the saturation point of the latter. The problem I propose to consider is their diversified relation to electrolytes. Connected with this problem is another, namely, the relation of solutions of globulins to colloidal solution. Do they form hydrosols at all, and, if so, to what extent? Krafft urged the colloidal nature of soap solutions, because, within certain limits of temperature and concentration, they gelatinise, and have the vapour pressure of pure water. Kahlenberg and Schreiner, however, regard soap solutions as being crystalloid in character, because over the whole range of concentration the soap is a good electrolyte—it ionises and undergoes hydrolytic splitting, like other salts of a weak acid and strong base. Smits, again, by measurement of the vapour pressure over a wide range of concentration, is convinced that above a critical concentration the soap passes wholly into the colloidal state.