[Purification and properties of inhibitor from vegetative portion of alfalfa].
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.
D000818:Animals; D001921:Brain / Q000201:enzymology; D002402:Cathepsin D; D002403:Cathepsins / Q000378:metabolism; D002417:Cattle; D002846:Chromatography, Affinity; D007700:Kinetics; D000455:Medicago sativa / Q000032:analysis; D008970:Molecular Weight; D010944:Plants / Q000032:analysis*; D014361:Trypsin Inhibitors / Q000302:isolation & purification* / Q000494:pharmacology
D014361:Trypsin Inhibitors; D002403:Cathepsins; D002402:Cathepsin D
Ochistka i nekotorye svoĭstva ingibitora tripsina iz vegetativnykh organov liutserny.