Zobrazeno 1 - 10
of 29
pro vyhledávání: '"E S, Oksenoit"'
Autor:
Irina A. Goptar, Yakov E. Dunaevsky, Tatiana A. Semashko, D. P. Zhuzhikov, Elena N. Elpidina, E. N. Lysogorskaya, Brenda Oppert, I. Yu. Filippova, Mikhail A. Belozersky, S.A. Danilenko, E. S. Oksenoit
Publikováno v:
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 161:148-154
article i nfo Article history: The major storage proteins in cereals, prolamins, have an abundance of the amino acids glutamine and proline. Storage pests need specific digestive enzymes to efficiently hydrolyze these storage proteins. Therefore, pos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57fbf025779c26d0eb35190e01ef8691
https://doi.org/10.1016/j.cbpb.2011.10.005
https://doi.org/10.1016/j.cbpb.2011.10.005
Proteinase-catalyzed peptide synthesis in concentrated solutions of urea and other denaturing agents
Autor:
Anisimova Vv, Valentin M. Stepanov, S. V. Kolobanova, E. S. Oksenoit, Irina Yu. Filippova, E. N. Lysogorskaya
Publikováno v:
International Journal of Peptide and Protein Research. 47:28-35
Pepsin successfully catalyzed the synthesis of several hydrophobic octa- and decapeptides in dimethylformamide-water solutions containing concentrated urea at pH 4.65. The factors that influence peptide synthesis in the presence of urea aere studied
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45832193b6a3a54e1fb4dc415282315e
https://doi.org/10.1111/j.1399-3011.1996.tb00806.x
https://doi.org/10.1111/j.1399-3011.1996.tb00806.x
Publikováno v:
ResearcherID
A chemoenzymatic syntheses was developed for new highly specific fluorogenic substrates for cysteine proteases of the papain family, Abz-Phe-Ala-pNA (I) and Glp-Phe-Ala-Amc (II) (Abz, pNA, Glp, and Amc are i-aminobenzoyl, p-nitroanilide, pyroglutamyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2d86d53c668b39cfc8ac70fbaea48db
https://doi.org/10.1134/s1068162008030151
https://doi.org/10.1134/s1068162008030151
Autor:
I. A. Koulemzina, Ya. E. Dunaevsky, D. P. Zhuzhikov, E. S. Oksenoit, Elena N. Elpidina, I. Yu. Filippova, E. N. Lysogorskaya, Irina A. Goptar, Mikhail A. Belozersky
Publikováno v:
Russian Journal of Bioorganic Chemistry. 34:280-285
Two post-proline cleaving enzymes PRE1 and PRE2 with molecular masses of 101 and 62 kDa, respectively, capable of hydrolyzing Z-AlaAlaPro-pNA were isolated for the first time from the midgut of the flour beetle Tenebrio molitor and characterized. PRE
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7309e66741f5179e79d1b8c091222ff1
https://doi.org/10.1134/s1068162008030047
https://doi.org/10.1134/s1068162008030047
Publikováno v:
Russian Journal of Bioorganic Chemistry. 32:116-121
The activity and stability of native subtilisin Karlsberg and subtilisin 72 and their complexes with sodium dodecyl sulfate (SDS) in organic solvents were studied. The kinetic constants of the hydrolysis of specific chromogenic peptide substrates Z-A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d91b2d08f5f7a2bd21e559c3c753b18a
https://doi.org/10.1134/s1068162006020026
https://doi.org/10.1134/s1068162006020026
Autor:
E. S. Oksenoit, Irina Yu. Filippova, Anastasiya V. Belyaeva, E. N. Lysogorskaya, Vladimir I. Lozinsky, A. V. Bacheva
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 32:253-260
Subtilisin 72 was immobilized on cryogel of poly(vinyl alcohol), the macroporous carrier prepared by the freeze-thaw-treatment of concentrated aqueous solution of the polymer. The obtained biocatalyst was active and stable in aqueous, aqueous-organic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f5a27f75d879b1662ac1adc86d5a3332
https://doi.org/10.1016/j.molcatb.2004.12.009
https://doi.org/10.1016/j.molcatb.2004.12.009
Autor:
T. I. Velichko, A. V. Bacheva, Alexander K. Gladilin, E. N. Lysogorskaya, A. V. Belyaeva, Vladimir I. Lozinsky, O. V. Baibak, E. S. Oksenoit, I. Yu. Filippova
Publikováno v:
Biochemistry (Moscow). 68:1261-1266
The activity and stability of native subtilisin 72, its complex with poly(acrylic acid), and subtilisin covalently attached to poly(vinyl alcohol) cryogel were studied in aqueous and organic media by hydrolysis of specific chromogenic peptide substra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bca2c7a162108abb841da1f0288abc9
https://doi.org/10.1023/b:biry.0000009142.88974.85
https://doi.org/10.1023/b:biry.0000009142.88974.85
Autor:
O. V. Baibak, A. V. Belyaeva, A. V. Bacheva, I. Yu. Filippova, V. I. Lozinskii, E. N. Lysogorskaya, E. S. Oksenoit
Publikováno v:
Russian Journal of Bioorganic Chemistry. 29:502-508
The catalytic efficiencies of native subtilisin, its noncovalent complex with polyacrylic acid, and the subtilisin covalently immobilized in a cryogel of polyvinyl alcohol were studied in the reaction of peptide coupling in mixtures of organic solven
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a2a664b940cf94a6d366325e22b7bb03
https://doi.org/10.1023/a:1026013912147
https://doi.org/10.1023/a:1026013912147
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 15:105-110
The role of acyl donor structure on the course of peptide bond formation catalyzed by SDS-subtilisin in ethanol was investigated. In the reaction ZAlaAlaLeuOR+HPhepNA→ZAlaAlaLeuPhepNA, nearly quantitative product yi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0f8f9708d87807c483626ca03e28addc
https://doi.org/10.1016/s1381-1177(01)00013-3
https://doi.org/10.1016/s1381-1177(01)00013-3
Autor:
I. Yu. Filippova, A. V. Bacheva, E. N. Lysogorskaya, S. V. Kolobanova, Valentin M. Stepanov, E. S. Oksenoit
Publikováno v:
Russian Journal of Bioorganic Chemistry. 27:306-310
The segment condensation of peptides on a solid phase (Aminosilochrom) in organic medium catalyzed by a subtilisin complex with sodium dodecylsulfate was studied. The dependence of the efficiency of the enzymatic coupling of tripeptides with the basi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aa4d16fc020ef0025c36a8207e6f104d
https://doi.org/10.1023/a:1012388229945
https://doi.org/10.1023/a:1012388229945