Zobrazeno 1 - 10
of 52
pro vyhledávání: '"D I, Metelitza"'
Publikováno v:
Scopus-Elsevier
The inhibition efficiency (antioxidant activity) of hydroxy derivatives of coumarin, such as esculetin, dicumarol, and fraxetin, was studied in the methemalbumin-H2O2-tetramethylbenzidine (TMB) pseudoperoxidase system at 20°C in a buffered physiolog
Publikováno v:
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry. 3:71-76
A comparative kinetic study of the inhibition of urea hydrolysis by 9 substituted 1,5,6,7-tetrahydro-4H-benzimidazol-4-ones (BI I–IX) has been carried out. The inhibition had reversible competitive mode; the inhibition constants Ki, varied from 29
Publikováno v:
Applied Biochemistry and Microbiology. 44:19-27
Effect of 2-acylcyclohexane-1,3-dione derivatives (tralkoxydim and its diketone precursors) on peroxidase-catalyzed oxidation of 3,3′,5,5′-tetramethylbenzidine (TMB), o-phenylenediamine (PDA), and the phenol-4-aminoantipyrine (4-AAP) couple has b
Publikováno v:
Applied Biochemistry and Microbiology. 43:139-149
Seven structurally diverse flavonoids have been shown to decrease glucose-6-phosphate dehydrogenase (G6PDH) inactivation in 0.1 M phosphate buffer (pH 7.4), induced by exposure to a high temperature (44°C), or by a low-frequency ultrasound (27 kHz,
Autor:
E. I. Karaseva, D. I. Metelitza
Publikováno v:
Russian Journal of Bioorganic Chemistry. 32:436-443
The inactivation kinetics of glucoso-6-phosphate dehydrogenase (GPDH) and its complexes with glucoso-6-phosphate and NADP+ was characterized in aqueous solutions at 36–47°C under treatment with low frequency (27 kHz, 60 W/cm2) and high frequency u
Publikováno v:
Biochemistry (Moscow). 69:1344-1352
Competitive inhibition of soybean urease by 15 triketone oximes has been studied at 36°C in aqueous solution (pH 4.95). The studied oximes are supposed chelators for the nickel atom in the urease metallocenter. The inhibition constants of urea hydro
Publikováno v:
Applied Biochemistry and Microbiology. 40:337-344
Competitive inhibition of soybean urease by 11 cyclic β-triketones was studied in aqueous solutions at pH 7.4 and 36°C. This process was characterized quantitatively by the inhibition constant (Ki), which showed a strong dependence on the structure
Publikováno v:
Russian Journal of Bioorganic Chemistry. 30:283-290
The peroxidase-catalyzed oxidation of 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS), o-phenylenediamine (PDA), and 3,3′,5,5′-tetramethylbenzidine (TMB) was found to be activated by tetrazole and 5-aminotetrazole (AT) and weakly i
Publikováno v:
Applied Biochemistry and Microbiology. 39:352-362
Peroxidase-catalyzed oxidation of o-phenylene diamine (OPD) was competitively inhibited by trimethylhydroquinone (TMHQ), 4-tert-butylpyrocatechol (InH5), and 4,6-di-tert-butyl-3-sulfanyl-1,2-dihydroxybenzene (InH6). InH6 was the most efficient inhibi
Publikováno v:
Biochemistry (Moscow). 68:54-62
The peroxidase-catalyzed oxidation of 3,3",5,5"-tetramethylbenzidine (TMB), ortho-phenylenediamine (PDA), and 5-aminosalicylic acid (5-ASA) is significantly accelerated in the presence of 2-aminothiazole (AT) and melamine (MA), and an increase in the