Human leukocyte elastase inhibition by Bowman-Birk soybean inhibitor. Discrimination of the inhibition mechanisms

Larionova, N.I.; Gladysheva, I.P.; Gladyshev, D.P.

FEBS Letters 404(2-3): 245-248

1997


ISSN/ISBN: 0014-5793
PMID: 9119072
DOI: 10.1016/s0014-5793(97)00089-6
Accession: 008788952

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Abstract
The reaction between human leukocyte elastase and soybean Bowman-Birk inhibitor has been studied. The inhibition was found to be due to slow tight binding of the inhibitor. The interaction of BBI with HLE was shown to involve two steps: the rapid formation of an initial EI complex, with a Ki of 28 nM, followed by a slow equilibrium conversion to a tighter-binding EI* complex with a final Ki* of 2.3 nM. At pH 7.5 and 25 degrees C, k(on) was 3.5 x 10(4) M(-1) s(-1) and k(off) was 1.0 x 10(-4) s(-1).