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  • Title: Kinetics of interaction of trypsin with an anionic inhibitor of trypsin BWI-1a from buckwheat seeds.
    Author: Gladysheva IP, Gladyshev DP, Dunaevsky YE, Belozersky MA, Larionova NI.
    Journal: Biochemistry (Mosc); 1999 Oct; 64(10):1104-7. PubMed ID: 10561554.
    Abstract:
    The kinetics of binding of bovine trypsin to a proteinaceous inhibitor of trypsin from buckwheat seeds (BWI-1a) has been studied. The association rate constant (k(ass)) was 2.2 x 10(6) M-1 x sec-1 and the dissociation rate constant (k(off)) of the enzyme--inhibitor complex was 3.5 x 10(-3) sec-1; the inhibition constant Ki was 1.5 nM. The inhibitor BWI-1a is of the slow, tightly binding type. The mechanism of the inhibition of bovine trypsin by the trypsin inhibitor BWI-1a was studied. The mechanism of inhibition was found to involve two steps according to the kinetic data.
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