Purification and Characterization of a Proteinase Inhibitor from Lolium perenne L.

A proteinase inhibitor from dry seeds of Lolium perenne L. cv. Grasslands Ruanui has been partially purified and characterised. Standard protein separalion techniques have been used to enrich the presence of lhe inhibitor in seed extracts by 37-fold. Using synthetic substrates the inhibitor can retard the activity of bovine chymotrypsin, but not bovine trypsin. Gel filtration column chromatography indicates that the native protein has a molecular weight of c. 20 KDa.