[Trypsin inhibitor from Amaranth (Amaranthys cruentus) leaves].
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.
Ievleva
E V
EV
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
Rudenskaia
Iu A
IuA
Zimacheva
A V
AV
Mosolov
V V
VV
D006868:Hydrolysis; D007700:Kinetics; D019684:Magnoliopsida; D014361:Trypsin Inhibitors / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism
D014361:Trypsin Inhibitors