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Paper Information

Journal:   DARU JOURNAL OF PHARMACEUTICAL SCIENCE   2004 , Volume 12 , Number 4; Page(s) 165 To 169.
 
Paper: 

KINETIC CHARACTERIZATION OF HK6 INHIBITION BY PROTEASE INHIBITOR, SOYBEAN

 
 
Author(s):  AWSAT MELLATI A.*, ELEFTHERIOS E., DIAMENDIS P.
 
* DEPARTMENT OF BIOCHEMISTRY, ZANJAN MEDICAL SCHOOL, IRAN
 
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.

 
Keyword(s): HK6, TRYPSIN, SOYBEAN, KINETIC, INHIBITION
 
References: 
 
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