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[Trypsin inhibitor from Amaranth (Amaranthys cruentus) leaves]
E V Ievleva1, Iu A Rudenskaia, A V Zimacheva
1Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
Prikladnaia Biokhimiia I Mikrobiologiia
|October 24, 2000
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.