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Pregled bibliografske jedinice broj: 688836

A study of the inhibition of catalase by dipotassium trioxohydroxytetrafluorotriborate K2[B3O3F4OH]


Islamović, Safija; Galić, Borivoj; Miloš, Mladen;
A study of the inhibition of catalase by dipotassium trioxohydroxytetrafluorotriborate K2[B3O3F4OH] // Journal of enzyme inhibition and medicinal chemistry, 29 (2014), 5; 744-748 doi:10.3109/14756366.2013.848203 (međunarodna recenzija, članak, znanstveni)


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Naslov
A study of the inhibition of catalase by dipotassium trioxohydroxytetrafluorotriborate K2[B3O3F4OH]

Autori
Islamović, Safija ; Galić, Borivoj ; Miloš, Mladen ;

Izvornik
Journal of enzyme inhibition and medicinal chemistry (1475-6366) 29 (2014), 5; 744-748

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
boroxine; catalase; drug research; enzyme inhibition

Sažetak
In the development of boronic acid-based enzyme inhibitors as potential pharmaceutical drugs, dipotassium trioxohydroxytetrafluorotriborate K2[B3O3F4OH] was listed as a promising new therapeutic for treatment of different diseases. The catalase-mediated conversion of hydrogen peroxide, in the presence and absence of K2[B3O3F4OH] was studied. The kinetics conformed to the Michaelis–Menten model. Lineweaver–Burk plots were linear and plotted the family of straight lines intersected on the abscissa indicating non-competitive inhibition of the catalase. It appears that in the absence of inhibitor, catalase operates the best at conditions around pH 7.1 and in the presence of K2[B3O3F4OH] the optimum is around pH 6.2. The uncatalyzed reaction of hydrogen peroxide decomposition generally has a value of activation energy of 75 kJ mole−1, whereas catalase, in the absence of inhibitor, lowers the value to 11.2 kJ  mole−1, while in the presence 69 mmoles L−1 of K2[B3O3F4OH] it was 37.8 kJ mole−1.

Izvorni jezik
Engleski

Znanstvena područja
Kemija



POVEZANOST RADA


Projekti:
011-2160547-1330 - Antioksidacijski sastojci i inhibitori kolinesteraza iz aromatičnog bilja (Miloš, Mladen, MZOS ) ( CroRIS)

Ustanove:
Kemijsko-tehnološki fakultet, Split

Profili:

Avatar Url Mladen Miloš (autor)

Poveznice na cjeloviti tekst rada:

doi www.tandfonline.com

Citiraj ovu publikaciju:

Islamović, Safija; Galić, Borivoj; Miloš, Mladen;
A study of the inhibition of catalase by dipotassium trioxohydroxytetrafluorotriborate K2[B3O3F4OH] // Journal of enzyme inhibition and medicinal chemistry, 29 (2014), 5; 744-748 doi:10.3109/14756366.2013.848203 (međunarodna recenzija, članak, znanstveni)
Islamović, S., Galić, B., Miloš, M. & (2014) A study of the inhibition of catalase by dipotassium trioxohydroxytetrafluorotriborate K2[B3O3F4OH]. Journal of enzyme inhibition and medicinal chemistry, 29 (5), 744-748 doi:10.3109/14756366.2013.848203.
@article{article, author = {Islamovi\'{c}, Safija and Gali\'{c}, Borivoj and Milo\v{s}, Mladen}, year = {2014}, pages = {744-748}, DOI = {10.3109/14756366.2013.848203}, keywords = {boroxine, catalase, drug research, enzyme inhibition}, journal = {Journal of enzyme inhibition and medicinal chemistry}, doi = {10.3109/14756366.2013.848203}, volume = {29}, number = {5}, issn = {1475-6366}, title = {A study of the inhibition of catalase by dipotassium trioxohydroxytetrafluorotriborate K2[B3O3F4OH]}, keyword = {boroxine, catalase, drug research, enzyme inhibition} }
@article{article, author = {Islamovi\'{c}, Safija and Gali\'{c}, Borivoj and Milo\v{s}, Mladen}, year = {2014}, pages = {744-748}, DOI = {10.3109/14756366.2013.848203}, keywords = {boroxine, catalase, drug research, enzyme inhibition}, journal = {Journal of enzyme inhibition and medicinal chemistry}, doi = {10.3109/14756366.2013.848203}, volume = {29}, number = {5}, issn = {1475-6366}, title = {A study of the inhibition of catalase by dipotassium trioxohydroxytetrafluorotriborate K2[B3O3F4OH]}, keyword = {boroxine, catalase, drug research, enzyme inhibition} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


Citati:





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