PURIFICATION AND CHARACTERIZATION OF PISUM SEED TRYPSIN-INHIBITORS

Seed trypsin inhibitors have been purified from Pisum. Three groups of inhibitor were separated using column chromatography, whereas non-den aturing activity gels showed that five inhibitors could be distinguish ed. N-terminal sequence data obtained for two purified inhibitors show ed that these belong to the Bowman-Birk class of inhibitors. Partial p urification and characterization of a protease with in vitro trypsin-l ike activity from Pisum seed protein preparations indicated that this endogenous protease is not inhibited by any of the fractionated inhibi tors.