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Information Journal Paper

Title

KINETIC CHARACTERIZATION OF HK6 INHIBITION BY PROTEASE INHIBITOR, SOYBEAN

Pages

  165-169

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.

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    Cite

    APA: Copy

    AWSAT MELLATI, A., ELEFTHERIOS, E., & DIAMENDIS, P.. (2004). KINETIC CHARACTERIZATION OF HK6 INHIBITION BY PROTEASE INHIBITOR, SOYBEAN. DARU JOURNAL OF PHARMACEUTICAL SCIENCE, 12(4), 165-169. SID. https://sid.ir/paper/275228/en

    Vancouver: Copy

    AWSAT MELLATI A., ELEFTHERIOS E., DIAMENDIS P.. KINETIC CHARACTERIZATION OF HK6 INHIBITION BY PROTEASE INHIBITOR, SOYBEAN. DARU JOURNAL OF PHARMACEUTICAL SCIENCE[Internet]. 2004;12(4):165-169. Available from: https://sid.ir/paper/275228/en

    IEEE: Copy

    A. AWSAT MELLATI, E. ELEFTHERIOS, and P. DIAMENDIS, “KINETIC CHARACTERIZATION OF HK6 INHIBITION BY PROTEASE INHIBITOR, SOYBEAN,” DARU JOURNAL OF PHARMACEUTICAL SCIENCE, vol. 12, no. 4, pp. 165–169, 2004, [Online]. Available: https://sid.ir/paper/275228/en

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