Purification and characterization of protease inhibitors from peanuts (Arachis hypogaea).
Five protease inhibitors were isolated from peanut seeds and named A-I, A-II, B-I, B-II, and B-III. These inhibitors seemed to be Bowman-Birk type inhibitors judging from their low molecular weights and high cystine contents. All the inhibitors inhibited both bovine trypsin and chymotrypsin at ratios of 1:2 and 1:1, respectively, but not simultaneously. The complexes of the inhibitors and trypsin no longer inhibit chymotrypsin. On the other hand, their complexes with chymotrypsin inhibit trypsin with a slow release of chymotrypsin.
D000596:Amino Acids / Q000032:analysis; D010367:Arachis / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D011480:Protease Inhibitors / Q000302:isolation & purification* / Q000494:pharmacology; D014361:Trypsin Inhibitors / Q000302:isolation & purification
D000596:Amino Acids; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D002918:Chymotrypsin