Abstract
The permeability of gelatin-coated collodion membranes, as measured by the flow of water or of dilute solutions through the membranes, has been found to vary with the pH of the solutions. The permeability is greatest near the isoelectric point of the protein; with increasing concentration of either acid or alkali it decreases, passes through a minimum, and then increases. These variations with pH are qualitatively in accord with the assumption that they are due to swelling of the gelatin in the pores of the membrane, the effects of pH being similar to those observed by Loeb on the swelling of gelatin granules. Indications have been found of a similar variable permeability in the case of membranes coated with egg albumin, edestin, serum euglobulin, and serum albumin.