E
E. N. Lysogorskaya
Researcher at Moscow State University
Publications - 36
Citations - 446
E. N. Lysogorskaya is an academic researcher from Moscow State University. The author has contributed to research in topics: Subtilisin & Peptide synthesis. The author has an hindex of 10, co-authored 36 publications receiving 427 citations.
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Journal ArticleDOI
L-Pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide--a chromogenic substrate for thiol proteinase assay.
I. Yu. Filippova,E. N. Lysogorskaya,E. S. Oksenoit,Galina N. Rudenskaya,Valentin M. Stepanov +4 more
TL;DR: This substrate was successfully applied to monitor thiol proteinase affinity chromatography on bacitracin-Sepharose, which resulted in a 2- to 4-fold purification from commercial preparations.
Journal ArticleDOI
A serine proteinase of an archaebacterium, Halobacterium mediterranei. A homologue of eubacterial subtilisins
Valentin M. Stepanov,Galina N. Rudenskaya,L P Revina,Y B Gryaznova,E. N. Lysogorskaya,Filippova IYu,I I Ivanova +6 more
TL;DR: The serine proteinase secreted by the halophilic bacterium should be considered as a functional analogue, and a structural homologue, of eubacterial serineproteinases (subtilisins), indicating that the enzyme belongs to the subtilisin family.
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Peptide synthesis in organic media with subtilisin 72 immobilized on poly(vinyl alcohol)-cryogel carrier.
TL;DR: Serine proteinase subtilisin 72 was covalently attached to the beads of poly(vinyl alcohol)-cryogel, a macroporous hydrogel prepared by the freeze-thaw technique and catalyzed with high yield the formation of peptide bonds between Phe-pNA and acyl donors.
Journal ArticleDOI
Fluorogenic Peptide Substrates for Assay of Aspartyl Proteinases
Irina Yu. Filippova,E. N. Lysogorskaya,Anisimova Vv,Leonid I. Suvorov,E. S. Oksenoit,Valentin M. Stepanov +5 more
TL;DR: Via a combination of chemical and enzymatic synthesis, new hexapeptide substrates convenient for use in activity assessment of several aspartyl proteinases--porcine pepin, human pepsin, gastricsin, and cathepsin D--were prepared.
Journal ArticleDOI
Cysteine digestive peptidases function as post-glutamine cleaving enzymes in tenebrionid stored-product pests
Irina A. Goptar,Tatiana A. Semashko,S.A. Danilenko,E. N. Lysogorskaya,E. S. Oksenoit,D. P. Zhuzhikov,Mikhail A. Belozersky,Yakov E. Dunaevsky,Brenda Oppert,I. Yu. Filippova,Elena N. Elpidina +10 more
TL;DR: It is proposed that the evolutionary conservation of cysteine peptidase in the complement of digestive peptidases of tenebrionid stored-product beetles is due not only to the adaptation of insects to plants rich in serine peptide inhibitors, but also to accommodate the need to efficiently cleave major dietary proteins rich in glutamine.