title: [Trypsin inhibitor from Amaranth (Amaranthys cruentus) leaves].
abstract: A protein that inhibited the proteolytic activity of trypsin was isolated from amaranth leaves (Amaranthus cruentus) by affinity chromatography on trypsin-Sepharose. The inhibition was noncompetitive (with n-nitroanilide-N-alpha-benzoyl-DL-arginine as substrate) and had a Ki of 11.87 x 10(-7) 7 M. The protein caused a weaker inhibitory effect on chymotrypsin, had no effect on subtilisin, displayed a molecular weight of 8 kDa, and contained no cysteine residues.
authors.affiliation: Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
authors.forename: E V
authors.initials: EV
authors.lastname: Ievleva
authors.forename: Iu A
authors.initials: IuA
authors.lastname: Rudenskaia
authors.forename: A V
authors.initials: AV
authors.lastname: Zimacheva
authors.forename: V V
authors.initials: VV
authors.lastname: Mosolov
mesh_terms: D006868:Hydrolysis; D007700:Kinetics; D019684:Magnoliopsida; D014361:Trypsin Inhibitors / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D014361:Trypsin Inhibitors