Zobrazeno 1 - 10
of 19
pro vyhledávání: '"E. I. Tarun"'
Publikováno v:
AIP Conference Proceedings.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::77330956fb5b0a460ec99e4cb001252b
https://doi.org/10.1063/5.0069049
https://doi.org/10.1063/5.0069049
Peptide composition, antioxidant activity, antimutagenic action and antimicrobial potential of defatted and fermented colostrum were compared. In colostrum samples fermented with Lactobacillus acidophilus the relative amount of fraction with a molecu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aabf074fba9e08d35fd5d26dc7a2310c
https://elib.belstu.by/handle/123456789/56666
https://elib.belstu.by/handle/123456789/56666
Autor:
E. I. Tarun, Т. M. Halavach, N. V. Dudchik, Vladimir P. Kurchenko, R. V. Romanovich, I. A. Bubra
Publikováno v:
Proceedings of the National Academy of Sciences of Belarus, Biological Series. 63:409-418
Antioxidant, antimutagenic and antigenic properties of partial hydrolysates of whey and colostrum obtained using bacterial endopeptidase (alcalase) have been investigated. It was found that the depth of proteolysis, qualitative and quantitative compo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f4a37ac79366f5c9a70fa1c47a5f19c6
https://doi.org/10.29235/1029-8940-2018-63-4-409-418
https://doi.org/10.29235/1029-8940-2018-63-4-409-418
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ccd1144b271e7d4a4046f99a995ae00d
https://doi.org/10.1134/s1990750809010107
https://doi.org/10.1134/s1990750809010107
Publikováno v:
Applied Biochemistry and Microbiology. 45:9-16
The inactivation of Aspergillus niger glucose oxidase (GO) was studied in 0.02 M phosphate-citrate buffer (PCB) at various pH, temperatures of 37–59°C, and sonication with low frequency (27 kHz, LF-US) and high frequency (2.64 MHz, HF-US) ultrasou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a46b0ee050a7327cefb973027145b74a
https://doi.org/10.1134/s0003683809010025
https://doi.org/10.1134/s0003683809010025
Publikováno v:
Applied Biochemistry and Microbiology. 41:12-17
Competitive inhibition of soybean urease was studied at 36°C in aqueous solution (pH 4.95) in the presence of polycarbonyl compounds (PCCs): oxalyldihydrazide (ODH), its polydisulfide (poly(DSODH)), three cyclic β-triketones (CTKs), and seven cycli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e04e599cbcdd31a806a5d34437c79855
https://doi.org/10.1007/s10438-005-0003-y
https://doi.org/10.1007/s10438-005-0003-y
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c284c6414bb20ed9f1ef7faab765a9ec
https://doi.org/10.1007/s10541-005-0079-2
https://doi.org/10.1007/s10541-005-0079-2
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9962674cbd5e74bcf1f33943229a2f18
https://doi.org/10.1023/b:abim.0000033908.87711.b5
https://doi.org/10.1023/b:abim.0000033908.87711.b5
Publikováno v:
Applied Biochemistry and Microbiology. 38:509-516
Inactivation of urease (25 nM) in aqueous solutions (pH 5.0–6.0) treated with low-frequency ultrasound (LFUS; 27 kHz, 60 W/cm2, 36–56°C) or high-frequency ultrasound (HFUS; 2.64 MHz, 1 W/cm2, 36 or 56°C) has been characterized quantitatively, u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1e5b2325303771411d08b9fc7305860c
https://doi.org/10.1023/a:1020759224487
https://doi.org/10.1023/a:1020759224487
Publikováno v:
Applied Biochemistry and Microbiology. 37:168-173
Inhibition of soybean urease by polymeric substrate analogues, urea and thiourea polydisulfides (PDSU and PDSTU, respectively); or three thiophosphoric acid amides (TPAA), tri-(N-3-hydroxyphenyl)thiophosphamide (1), tri-(N-4,4"-aminodiphenyl)thiophos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9699321bf9c6f0805c6237036993d2c4
https://doi.org/10.1023/a:1002879815168
https://doi.org/10.1023/a:1002879815168