Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Vladimir A. Yurshev"'
Autor:
Alexey Yu. Plesovskikh, Svetlana E. Krylova, Vladimir I. Yurshev, Andrey A. Seregin, Ivan A. Kurnoskin
Publikováno v:
Key Engineering Materials. 910:464-471
The results of a technological process development for obtaining a wear-resistant powder coating of Ni-Mo-Al system, applied by cold gas-flame spraying to the surface of a critical unit of compressor equipment in the oil and gas industry, within the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a993184b9bbfa49678f518f1a3fb677d
https://doi.org/10.4028/p-1k1vx0
https://doi.org/10.4028/p-1k1vx0
Autor:
Vladimir A. Yurshev, German A. Kochetov, Vitalii A. Selivanov, Olga N. Solovjeva, Irina A. Sevostyanova
Publikováno v:
The Protein Journal. 31:137-140
Catalytic activity has been demonstrated for holotransketolase in the absence of free bivalent cations in the medium. The two active centers of the enzyme are equivalent in both the catalytic activity and the affinity for the substrates. In the prese
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::588ec505854ca0d83d2c2018c3178088
https://doi.org/10.1007/s10930-011-9382-5
https://doi.org/10.1007/s10930-011-9382-5
Publikováno v:
Biochemistry (Moscow). 75:1014-1016
The effect of hexacyanoferrate(III) on the catalytic activity of transketolase has been studied. This oxidant inactivates only one of two active sites of the enzyme, the one with a higher affinity to the coenzyme (thiamine diphosphate). The second ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67be95698d41469b9e2df57507ad15ea
https://doi.org/10.1134/s0006297910080092
https://doi.org/10.1134/s0006297910080092
Autor:
Olga N, Solovjeva, Irina A, Sevostyanova, Vladimir A, Yurshev, Vitalii A, Selivanov, German A, Kochetov
Publikováno v:
The protein journal. 31(2)
Catalytic activity has been demonstrated for holotransketolase in the absence of free bivalent cations in the medium. The two active centers of the enzyme are equivalent in both the catalytic activity and the affinity for the substrates. In the prese
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f83840e7cb4a60f6e58470f32e9b01a2
https://pubmed.ncbi.nlm.nih.gov/22210509
https://pubmed.ncbi.nlm.nih.gov/22210509
Autor:
Vladimir A. Yurshev, S. V. Zabrodskaya, Olga N. Solovjeva, Vitaly A. Selivanov, German A. Kochetov, Irina A. Sevostyanova
Publikováno v:
Biochemistry. Biokhimiia. 74(7)
Catalytic activity of two active sites of transketolase and their affinity towards the substrates (xylulose-5-phosphate and ribose-5-phosphate) has been studied in the presence of Ca2+ and Mg2+. In the presence of Ca2+, the active sites exhibit negat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbb0c8d100e6c9963cd0b421533ece61
https://pubmed.ncbi.nlm.nih.gov/19747100
https://pubmed.ncbi.nlm.nih.gov/19747100
Autor:
Olga N. Solovjeva, Svetlana V. Zabrodskaya, Vladimir A. Yurshev, German A. Kochetov, Irina A. Sevostyanova
Publikováno v:
Proteins. 71(2)
The effect of the type of the cation cofactor of transketolase (i.e., Ca2+ or Mg2+) on its interaction with xylulose 5-phosphate (donor substrate) has been studied. In the presence of magnesium, the active centers of the enzyme were functionally equi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9674812f18d723cbfe4eb00860e6540
https://pubmed.ncbi.nlm.nih.gov/18186462
https://pubmed.ncbi.nlm.nih.gov/18186462
Autor:
Vladimir A. Yurshev, Irina A. Sevostyanova, Svetlana V. Zabrodskaya, Olga N. Solovjeva, German A. Kochetov
Publikováno v:
Biochemical and biophysical research communications. 361(4)
The interaction of transketolase with its acceptor substrate, ribose 5-phosphate, has been studied. The active centers of the enzyme were shown to be functionally nonequivalent with respect to ribose 5-phosphate binding. Under the conditions where on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9ecf2b2c3cdbdf0ec89e78bf8f2f215
https://pubmed.ncbi.nlm.nih.gov/17681280
https://pubmed.ncbi.nlm.nih.gov/17681280