Purification and properties of inhibitor from vegetative portion of alfalfa
Sukhinin, V.N.; Berezin, V.A.; Novikov, I.F.; Reva, A.D.; Lagutenko, A.V.
Biokhimiia 46(7): 1183-1187
1981
ISSN/ISBN: 0320-9725 PMID: 7272346 Document Number: 173786
Trypsin inhibitor was isolated from the vegetative portion of alfalfa and purified 270-fold by affinity chromatography on Trypsin-Sepharose. The inhibitor was eluted by gel-filtration as a single peak with molecular weight of 6900. Disc-electrophoresis of the purified inhibitor revealed the presence of only one protein band. Trypsin inhibition is a mixed process. The trypsin inhibitor from alfalfa does not prevent the activity of cathepsin D from bovine brain. Trypsin inhibitor was immobilized on BrCN-activated Sepharose 4B. The binding of trypsin to the immobilized trypsin inhibitor was studied: 5 mg of the immobilized trypsin inhibitor were found to bind 1 mg of trypsin.