Abstract
The proteins of the zein complex from maize endosperm have been studied with the aid of hydrophobic chromatography. Their best separation was achieved on a column with TSK gel HW-65f. By comparing the results of fractionation by hydrophobic chromatography with those of electrophoresis, it was found that electrophoresis in PAAG under denaturing conditions separates the zein protein into groups according to their surface hydrophobicity. The most hydrophobic is the high-molecular-mass group of zein polypeptides.
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