Zobrazeno 1 - 10
of 11
pro vyhledávání: '"I. M. Artsukevich"'
Publikováno v:
Journal of Molecular Structure. :261-264
Steady-state and time-resolved fluorescences were studied in alcohol oxidase from methylotropic yeast in the presence of substrate (ethanol). The fluorescence decay was found to be non-exponential and to reflect the heterogeneity of the microenvironm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5b10f0cae5fb06fe04eb0c9f6df238c8
https://doi.org/10.1016/s0022-2860(96)09538-5
https://doi.org/10.1016/s0022-2860(96)09538-5
Publikováno v:
Journal of Molecular Structure. 349:5-8
The SERS spectra of alcohol oxidase from Pichia pastoris adsorbed on a silver electrode were obtained. The similarities and differences of these spectra with the SERS spectrum of free flavin adenine dinucleiotide were considered. The dependence of re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e2c9c90bbc7531d45ea85df5b1f2561a
https://doi.org/10.1016/0022-2860(95)08695-r
https://doi.org/10.1016/0022-2860(95)08695-r
Publikováno v:
Spectroscopy of Biological Molecules ISBN: 9789401041669
The aim of this work is an attempt to establish a correlation between the SERS signal of protein-bound flavin adenine dinucleotide (FAD) and the peculiarities of the structure and functional state of alcohol oxidase (AO) by SERS. The SERS spectra of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a1e801e6e7d44ababa19679d3c70ca4b
https://doi.org/10.1007/978-94-011-0371-8_65
https://doi.org/10.1007/978-94-011-0371-8_65
Publikováno v:
Spectroscopy of Biological Molecules ISBN: 9789401041669
Alcohol oxidase (AO) has intrinsic fluorescence with a quantum yield of 4.5%. This is the fluorescence of the tryptophan residues situated at low-polar sites of the protein globule. The short-wave position of the emission spectrum (331 nm) at λex=29
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cfa4862fc723a167b1d3dcd54ba1028e
https://doi.org/10.1007/978-94-011-0371-8_64
https://doi.org/10.1007/978-94-011-0371-8_64
Publikováno v:
Acta vitaminologica et enzymologica. 5(2)
The functional role of histidine and sulfhydryl groups of thiamine pyrophosphokinase (ATP: thiamine pyrophosphotransferase, E.C.2.7.6.2) has been studied by the methods of photooxidation and chemical modification by diethylpyrocarbonate (DEPC) and El
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::08880a318b386314c1a5b5b4f52c5c6d
https://pubmed.ncbi.nlm.nih.gov/6307024
https://pubmed.ncbi.nlm.nih.gov/6307024
Autor:
S Iu, Ostrovskiĭ, I M, Artsukevich
Publikováno v:
Biokhimiia (Moscow, Russia). 54(11)
The pattern of kinetic behaviour of ethanolamine (EA), an ethanol structural analog, in the alcohol dehydrogenase reaction has been studied. EA has been shown to manifest a mixed type inhibition versus ethanol and a noncompetitive behaviour towards t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5ef7ea0a5cba442b550cec8d2308cebe
https://pubmed.ncbi.nlm.nih.gov/2627556
https://pubmed.ncbi.nlm.nih.gov/2627556
Publikováno v:
Voprosy meditsinskoi khimii. 30(2)
Amount and reactivity of SH-groups in thiamine pyrophosphokinase from rat liver tissue were studied using the mercaptide-forming reagents HgCl2 and p-chloromercury-benzoate (pCMB). Two types of SH-groups were found: the first--readily accessible and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6139c0d4c83d5767bfdc61ae0744c4d1
https://pubmed.ncbi.nlm.nih.gov/6331000
https://pubmed.ncbi.nlm.nih.gov/6331000
Autor:
I M, Artsukevich
Publikováno v:
Biokhimiia (Moscow, Russia). 44(3)
The nucleotide specificity of thiamine pyrophosphokinase from rat liver was studied. The enzyme was found to possess a sufficiently wide substrate specificity. Any of the nucleotides can be a donor of the pyrophosphate groups for TDP biosynthesis at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5711c5aa29e01298960b240ae52d41c9
https://pubmed.ncbi.nlm.nih.gov/223671
https://pubmed.ncbi.nlm.nih.gov/223671
Publikováno v:
Biokhimiia (Moscow, Russia). 43(3)
The kinetic analysis of bisubstrate enzymatic reaction catalysed by electrophoretically homogenous thiamine pyrophosphokinase (EC 2.7.6.2), isolated from rat liver has been carried out. Kinetic studies of the initial rates in the absence of the produ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::678fbeaeeadd9b62ece21fda89511567
https://pubmed.ncbi.nlm.nih.gov/207357
https://pubmed.ncbi.nlm.nih.gov/207357
Publikováno v:
Voprosy meditsinskoi khimii. 23(2)
Thiamin pyrophosphokinase (TPK) (EC 2.7.6.2) was isolated and purified from rat liver tissue ion in exchange chromatography, rechromatography and gel filtration. The enzyme was purified 3000-fold with yield of 12%, it was homogenous in polyacrylamide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::aabb29c2158c804b224ffa70bce9d99c
https://pubmed.ncbi.nlm.nih.gov/18841
https://pubmed.ncbi.nlm.nih.gov/18841