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Publication Date
1993
Location
New Zealand
Description
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.
Citation
Tasneem, Mohammed; Cornford, C A.; McManus, M T.; and White, D W.R, "Purification and Characterization of a Proteinase Inhibitor from Lolium perenne L." (1993). IGC Proceedings (1985-2023). 4.
(URL: https://uknowledge.uky.edu/igc/1993/session32/4)
Included in
Agricultural Science Commons, Agronomy and Crop Sciences Commons, Plant Biology Commons, Plant Pathology Commons, Soil Science Commons, Weed Science Commons
Purification and Characterization of a Proteinase Inhibitor from Lolium perenne L.
New Zealand
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.
