Zobrazeno 1 - 10
of 117
pro vyhledávání: '"S. S. Savin"'
Autor:
M. K. Koshkina, E. P. Sergeyev, T. A. Fedorov, M. D. Shelomov, A. A. Pometun, S. S. Savin, V. I. Tishkov, D. L. Atroshenko
Publikováno v:
Moscow University Chemistry Bulletin. 78:69-75
Publikováno v:
Moscow University Chemistry Bulletin. 78:1-9
Autor:
A. A. Pometun, A. A. Shirokova, N. P. Galanicheva, L. A. Shaposhnikov, D. L. Atroshenko, E. V. Pometun, V. I. Tishkov, S. S. Savin
Publikováno v:
Moscow University Chemistry Bulletin. 78:20-27
Autor:
T. S. Iurchenko, A. A. Loginova, E. P. Sergeev, E. V. Pometun, V. I. Tishkov, S. S. Savin, A. A. Pometun
Publikováno v:
Moscow University Chemistry Bulletin. 78:42-53
Autor:
T. S. Iurchenko, S. B. Bolotova, A. A. Loginova, E. V. Pometun, S. S. Savin, A. A. Pometun, V. I. Tishkov
Publikováno v:
Moscow University Chemistry Bulletin. 77:330-339
Autor:
P. D. Parshin, U. A. Martysuk, D. L. Atroshenko, A. N. Popinako, S. S. Savin, E. B. Pometun, V. I. Tishkov, A. A. Pometun
Publikováno v:
Moscow University Chemistry Bulletin. 77:242-248
Autor:
V. S. Sedov, A. K. Martyanov, A. S. Altakhov, S. S. Savin, E. A. Dobretsova, I. A. Tiazhelov, D. G. Pasternak, I. A. Kaplunov, V. E. Rogalin, V. G. Ralchenko
Publikováno v:
Journal of Russian Laser Research. 43:503-508
Autor:
Konstantin M. Boyko, D. L. Atroshenko, A. Yu. Nikolaeva, Vladimir I. Tishkov, A. A. Pometun, S. S. Savin, S. A. Zubanova
Publikováno v:
Moscow University Chemistry Bulletin. 76:49-55
NAD+-dependent formate dehydrogenase from thermotolerant yeast Ogataea parapolymorpha DL-1 (OpaFDH, EC 1.2.1.2) with the additional N-terminal Gly residue and its double mutant OpaFDH_AD were overexpressed in E. coli cells. The enzyme yield was, resp
Autor:
N. P. Galanicheva, D. L. Atroshenko, Vladimir I. Tishkov, A. A. Pometun, P. D. Parshin, S. S. Savin, I. V. Uporov
Publikováno v:
Moscow University Chemistry Bulletin. 75:250-257
NAD(P)+-dependent formate dehydrogenase (FDH, EC 1.2.1.2.) is actively used in processes of chiral synthesis by oxidoreductases with systems of reduced cofactor regeneration. The efficient use of FDH in such systems requires simple and fast enzyme pu
Autor:
P. D. Parshin, U A Martysuk, D. L. Atroshenko, A. A. Pometun, S. S. Savin, Vladimir I. Tishkov, E. V. Pometun, S. Yu. Kleymenov
Publikováno v:
Biochemistry (Moscow). 85:575-582
Phenylacetone monooxygenase (EC 1.14.13.92, PAMО) catalyzes oxidation of ketones with molecular oxygen and NADPH with the formation of esters. PAMО is a promising enzyme for biotechnological processes. In this work, we generated genetic constructs