T. A. McGuire, E. M. Craine, and R. J. Dimler. Copyright 1960 by the American Association of Cereal Chemists, Inc.
The globulins in water extracts of corn were fractionated by ion-exchange chromatography on carboxymethylcellulose (CMC). To increase solubility of the proteins at low pH, phytate ions were removed before chromatography. Proteins were adsorbed on unbuffered columns of CMC at low pH and ionic strength (1% acetic acid) and were desorbed by stepwise increases in the ionic strength of the eluant at constant pH (2.8). Rechromatography of components established that a true fractionation was obtained. Under conditions used, the unadsorbed material contained a true protein fraction, along with most of the yellow pigments and the nucleic acids of the extract. Evidence for an active nuclease was found.