الفهرس 
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Abstract
Peanut (Arachis hypogaea L. variety Giza 5) seed contained 26.3 % crude ~rotein. This seed contained inhibitor which inhibited both trypsin and chymotrypsin. rhus, it would be referred to as peanut protease inhibitor.
Four different extractants were examined for extracting TIA. Although distilled ,yater was effective as the other three acidic extractants (20 mM HCI, 2.5% TCA md 50 mM acetic acid), the specific activity of TIA and CIA was the highest in 50 ~M acetic acid extract which was used for extracting the inhibitor for purification.
Preliminary experiment indicated that protein precipitating from 50 mM acetic lcid extract by acetone fractionation (between 50 and 70% acetone concentration) ~ntained most inhibitory activity. This step achieved about 3 fold increase in the eciftc activity with recovery of 70%.
Peanut protease inhibitor was purified to homogeneity through, acetic acid action, acetone fractionation (using the protein precipitating between 50 and Wo of acetone concentration), anion exchange chromatography on DEAEE:~ulose column, ctlromatography on hydroxyapatit column and molecular sieve omatography on Sephadex G-75 column.