The Isoelectric Point of Collagen

Abstract

The isoelectric point of collagen prepared from steer hide with a minimum alkaline treatment has been shown, by measurements of electrophoretic mobility, to be at pH 7.8 in buffers of ionic strength 0.005. It is suggested that the shift of the isoelectric point to pH 4.7 in the case of commercial gelatin and hide powder is due to some structural change in the protein caused by the alkaline treatment given these materials. © 1939, American Chemical Society. All rights reserved.