Pregled bibliografske jedinice broj: 868163
Inhibition of Horseradish Peroxidase Activity by Boroxine Derivative, Dipotassium- trioxohydroxytetrafluorotriborate K2[B3O3F4OH]
Inhibition of Horseradish Peroxidase Activity by Boroxine Derivative, Dipotassium- trioxohydroxytetrafluorotriborate K2[B3O3F4OH] // Journal of Chemistry, 2017 (2017), 1-7 doi:10.1155/2017/8134350 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 868163 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Inhibition of Horseradish Peroxidase Activity by Boroxine Derivative, Dipotassium- trioxohydroxytetrafluorotriborate K2[B3O3F4OH]
Autori
Ostojić, Jelena ; Herenda, Safija ; Galijasević, Semira ; Galic, Borivoj ; Miloš Mladen
Izvornik
Journal of Chemistry (2090-9063) 2017
(2017);
1-7
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
Horseradish peroxidase, enzyme inhibition, boroxine
Sažetak
Recently research shows that horseradish peroxidase, HRP, when combined with other compounds, is highly reactive toward different human tumour cells and that better understanding of catalytic mechanism and inhibition HPR could lead to a new targeted cancer therapy. Thus, the inhibition of HRP activity by dipotassium- trioxohydroxytetrafluorotriborate K2[B3O3F4OH] was investigated for possible explanation of previously observed antitumour activities of this promising drug. HRP activity was studied under steady-state kinetic conditions by a spectrophotometric method. In the absence of the inhibitor values of Km = 0.47 mM and Vmax = 0.34 mM min−1, respectively, were determined. The hydrogen peroxide H2O2 kinetic measurements show a competitive inhibition with the inhibition constant Km = 2.56 mM. The activation energy values were found to be very similar for both reactions ; in the absence of inhibitor activation energy was 17.7 kJ mol−1 and in the presence of inhibitor activation energy was 16.3 kJ mol−1. The values of Arrhenius constants were found to be different ; A = 4.635 s−1 was measured in the absence of inhibitor while in the presence of inhibitor Arrhenius constant was 1.745 s−1 showing that K2[B3O3F4OH] initiates conformational change in the structure of the HRP and subsequently reduces its activity.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
POVEZANOST RADA
Projekti:
HRZZ-IP-2014-09-6897 - Istraživanje bioaktivnih spojeva iz dalmatinskog bilja: njihov antioksidacijski karakter i utjecaj na enzimsku inhibiciju i zdravlje (BioActCom) (Miloš, Mladen, HRZZ - 2014-09) ( CroRIS)
Ustanove:
Kemijsko-tehnološki fakultet, Split
Profili:
Mladen Miloš
(autor)
Citiraj ovu publikaciju:
Časopis indeksira:
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus