ISOLATION AND CHARACTERIZATION OF PROTEIN BODIES FROM COTYLEDONS OF DRY LUPINUS-ALBUS SEEDS

A technique for preparative isolation in nonaqueous glycerol of pure a nd native protein bodies from white lupin seeds has been developed Act ivities of hydrolytic enzymes and trypsin inhibitors were studied in i solated protein bodies and cytoplasm. The specific activities of aspar tic proteinase, beta-N-acetylglucosaminidase, alpha-D-mannosidase, and acid phosphatase were much higher in the protein bodies, and aspartic proteinase activity was associated most closely with this fraction. T he specific activity of leucine aminopeptidase was much higher in the cytoplasm. The activity of trypsin inhibitors is comparable in the pro tein body and cytoplasmic fractions.