KINETIC CHARACTERIZATION OF hK6 INHIBITION BY PROTEASE INHIBITOR, SOYBEAN
Abstract
The kinetic characteristics, of interaction between hK6 (human Kallikrein) and soybean (BBI) , protease
inhibitor and antitumor agent , in the presence of substrate (Phenylalanine –Serine-Arginine)-(7-amino-4-
methyl-coumarin) (FSR-AMC) were investigated. The hK6 were found to bind soybean in two reversible
steps, by slow binding inhibition mechanism. The Ki of the first step binding was 13 nM and Ki* of the
second binding step was 1.6 nM. The microcopic rate constants were calculated as follows: 311 M-1.S-1
for k3
, 0.04×10-6 M-1.S-1 for k –3 , 0.2×10-6 S-1 for k 4 and 0.025×10-6 S-1 for k-4 respectively.The results suggested
that the interaction mechanism between hK6 and soybean was like that of trypsin with this inhibitor but with
rather lower inhibitory constants values.
inhibitor and antitumor agent , in the presence of substrate (Phenylalanine –Serine-Arginine)-(7-amino-4-
methyl-coumarin) (FSR-AMC) were investigated. The hK6 were found to bind soybean in two reversible
steps, by slow binding inhibition mechanism. The Ki of the first step binding was 13 nM and Ki* of the
second binding step was 1.6 nM. The microcopic rate constants were calculated as follows: 311 M-1.S-1
for k3
, 0.04×10-6 M-1.S-1 for k –3 , 0.2×10-6 S-1 for k 4 and 0.025×10-6 S-1 for k-4 respectively.The results suggested
that the interaction mechanism between hK6 and soybean was like that of trypsin with this inhibitor but with
rather lower inhibitory constants values.
Keywords
hK6, trypsin, soybean, inhibition,
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