Zobrazeno 1 - 10
of 131
pro vyhledávání: '"D I, Metelitsa"'
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
Autor:
D. I. Metelitsa, E. I. Karaseva
Publikováno v:
Applied Biochemistry and Microbiology. 43:481-505
The role of complexes containing oxygen or peroxide in monooxygenase systems and models thereof, as well as in peroxidase- and quasi-peroxidase-catalyzed processes, has been reviewed. Pathways of conversion of these intermediate complexes involving s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::20a00181f5980f42c0bf17f94664ede9
https://doi.org/10.1134/s000368380705002x
https://doi.org/10.1134/s000368380705002x
Publikováno v:
Applied Biochemistry and Microbiology. 41:529-537
The kinetics of inactivation of catalases from bovine liver (CAT), the fungus Penicillium piceum (CAT1), and the methylotrophic yeast Pichia pastoris (CAT2) was studied in phosphate buffer (pH 5.5 or 7.4) at 45 and 50°C or under the conditions of ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::233abcbaf86f8f81e0b618a85f456a44
https://doi.org/10.1007/s10438-005-0096-3
https://doi.org/10.1007/s10438-005-0096-3
Publikováno v:
Applied Biochemistry and Microbiology. 41:330-335
Peroxidase-catalyzed oxidation of 2,2′-azino-di-(3-ethyl-2,3-dihydrobenzthiazoline-6-sulfonate) (ABTS) was competitively inhibited by propyl gallate (PG) and its polydisulfide (PGPDS) at 20° C in 0.015 M phosphate-citrate buffer (pH 6.0). Under th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b46be7b84601a98a09a2ac9d06d9cb19
https://doi.org/10.1007/s10438-005-0056-y
https://doi.org/10.1007/s10438-005-0056-y
Publikováno v:
Applied Biochemistry and Microbiology. 41:129-138
Peroxidase-catalyzed oxidation of 2,2-azino-di(3-ethyl-benzthiazolydine-6-sulfonic acid) (ABTS) and 3,3',5,5'-tetramethylbenzidine (TMB) is activated by tetrazole and its 5-substituted derivatives--5-amino-(AmT), 5-methyl- (MeT), 5-phenyl- (PhT), and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::35e257b10627d855f27d1b41ed4ae40e
https://doi.org/10.1007/s10438-005-0022-8
https://doi.org/10.1007/s10438-005-0022-8
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:
Applied Biochemistry and Microbiology. 40:120-128
Kinetics of inactivation of glucose-6-phosphate dehydrogenase (G6PDH, EC 1.1.1.49) in 0.1 M phosphate buffer (pH 7.4) within temperature range from 36 to 50 degrees C was studied comparatively under conditions of exposure of enzyme solution to low-fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::97aeb7599cc495fc0425f3c0c310d3c1
https://doi.org/10.1023/b:abim.0000018913.59738.9a
https://doi.org/10.1023/b:abim.0000018913.59738.9a
Autor:
A. N. Eremin, Zh. N. Kashkan, N. V. Kovganko, D. I. Metelitsa, M. V. Potapovich, S. N. Krivenok
Publikováno v:
Chemistry of Natural Compounds. 40:71-74
The kinetics of catalase decomposition of H2O2 (50 mM) inhibited by the flavonolic glycoside astragalin (1) from the aerial part of Gymnocarpium dryopteris were studied. 1 (0.3-30 M) is a strong inhibitor of the catalase process and was tested as a c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d453f575df7d720c44b8a136de634329
https://doi.org/10.1023/b:conc.0000025471.16712.bf
https://doi.org/10.1023/b:conc.0000025471.16712.bf
Publikováno v:
Applied Biochemistry and Microbiology. 39:140-146
Kinetic patterns of sonication-induced inactivation of bovine liver catalase (CAT) were studied in buffer solutions (pH 4-11) within the temperature range from 36 to 55 degrees C. Solutions of CAT were exposed to low-frequency (20.8 kHz) ultrasound (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::30fc97fd5cdbd2816afea83a59088576
https://doi.org/10.1023/a:1022577611056
https://doi.org/10.1023/a:1022577611056
Publikováno v:
Applied Biochemistry and Microbiology. 38:151-158
Effects of pH, enzyme concentration, and various supplements on the catalytic activity, temperature stability, and secondary structure of horseradish peroxidase (HRP) were studied in diluted aqueous solutions. In 5.0 mM citrate-phosphate buffer (pH 4
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5c566dfb4bbfc65343976dd32772a5cf
https://doi.org/10.1023/a:1014362600722
https://doi.org/10.1023/a:1014362600722