Abstract: In this experiment,wheat germ globulin was fractionated,and the physicochemical and structural properties of the main fraction of wheat germ globulin were comprehensively studied. The results of experiments showed that 8S globulin is the major fraction of wheat germ globulin. Reduced SDS-PAGE revealed that wheat germ 8S globulin has two predominant bands (55.0 kD and 38.0～40.0 kD). It has a relatively high level of glutamic acid,arginine,aspartic acid and leucine,whereas cystine and methionine are lacking. CD spectra indicated that wheat germ 8S globulin is a protein rich in β-sheet structure (54.9 %),followed by random coil (25.3 %) and α-helical (19.8 %) structure.

Key words: wheat germ, 8S globulin, physico-chemical properties, secondary structure