Výsledky vyhledávání - "O A, Stepnaia"

[Detection of AlpA and AlpB lytic endopeptidase propeptides of Lysobacter sp. XL1 by sandwich-enzyme immunoassay based on monoclonal antibodies]

Autor: N V, Rudenko, I M, Tsfasman, O R, Latypov, L A, Ledova, L A, Krasovskaia, A P, Karatovskaia, F A, Brovko, N V, Vasil'eva, O A, Stepnaia

Publikováno v: Bioorganicheskaia khimiia. 40(3)

The extracellular lytic endopeptidases AlpA and AlpB of the bacterium Lysobacter sp. XL1 are highly homologous and synthesized as precursors consisting of signal peptide, propeptide and mature form. In this work, two monoclonal antibodies against pro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b25959b813f1326d90034763cacecdde
https://pubmed.ncbi.nlm.nih.gov/25898736

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[Effect of the proteolytic enzymes of Bacillus licheniformis and the lysoamidase of Lysobacter sp. XL1 on Proteus vulgaris and Proteus mirabilis]

Autor: L P, Riazanova, L A, Ledova, N V, Tsurikova, O A, Stepnaia, A P, Sinitsyn, I S, Kulaev

Publikováno v: Prikladnaia biokhimiia i mikrobiologiia. 41(5)

Preparations of culture liquid of three Bacullus licheniformis strains (S, 103, and 60.4) and the enzymatic preparation lysoamidase from culture liquid of Lysobacter sp. strain XL1 actively lysed preliminarily autoclaved cells of gram-negative bacter

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d10759f8902a8cfe0799c198d2d58b05
https://pubmed.ncbi.nlm.nih.gov/16240656

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[Mechanism of action of the extracellular bacteriolytic enzymes of Lysobacter sp. on gram-positive bacteria: role of the cell wall anionic polymers of the target bacteria]

Autor: O A, Stepnaia, E A, Begunova, I M, Tsfasman, E M, Tul'skaia, G M, Streshinskaia, I B, Naumova, I S, Kulaev

Publikováno v: Mikrobiologiia. 73(4)

The study of the extracellular bacteriolytic enzymes of Lysobacter sp. showed that they can efficiently hydrolyze the peptidoglycan of gram-positive bacteria provided that there is an electrostatic interaction of these enzymes with the cell wall anio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3551228b8ef335b2c7ee713071e937b1
https://pubmed.ncbi.nlm.nih.gov/15521173

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[The effect of the extracellular bacteriolytic enzymes of Lysobacter sp. on gram-negative bacteria]

Autor: E A, Begunova, O A, Stepnaia, I M, Tsfasman, I S, Kulaev

Publikováno v: Mikrobiologiia. 73(3)

The effect of the extracellular bacteriolytic enzymes of Lysobacter sp. on gram-negative bacteria was studied. These enzymes were found to be able to hydrolyze the peptidoglycan that was isolated from the gram-negative bacteria, the hydrolysis being

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d63aa9245a243a265263855e08b91509
https://pubmed.ncbi.nlm.nih.gov/15315224

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[Lytic action of lysoamidase from Xanthomonas sp. correlates with the presence of the target ribitol teichoic acids in the cell wall of gram-positive bacteria]

Autor: I S, Kulaev, I B, Naumova, G M, Streshinskaia, E M, Tul'skaia, O A, Stepnaia, A I, Severin, E A, Begunova

Publikováno v: Mikrobiologiia. 65(3)

Lysoamidase, a bacteriolytic complex from the culture liquid of Xanthomonas sp., hydrolyzed the cells walls of Staphylococcus aureus, Streptomyces chrysomallus, and Streptomyces azureus, which contain ribitol teichoic acids in addition to peptidoglyc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::abca71b5f8bcee8ff13c10ba910b0d47
https://pubmed.ncbi.nlm.nih.gov/8992241

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[Structure of an acidic polysaccharide found in a bacteriolytic complex of lysoamidase]

Autor: L M, Likhosherstov, S N, Senchenkova, Iu A, Knirel', A S, Shashkov, V N, Shibaev, O A, Stepnaia, I S, Kulaev

Publikováno v: Biokhimiia (Moscow, Russia). 60(6)

A structural study of an acidic polysaccharide, a component of the lysoamidase bacteriolytic complex has been carried out. Analysis of the monosaccharide composition of the original polysaccharide, of the product of carboxyl groups reduction and of t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::eea844924379c96a49c3cf0f333bcbc1
https://pubmed.ncbi.nlm.nih.gov/7654860

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[Features of secretion of bacteriolytic enzymes and polysaccharides in bacteria from the Pseudomonadaceae family]

Autor: N E, Chumak, O A, Stepnaia, T S, Chermenskaia, I S, Kulaev, M A, Nesmeianova

Publikováno v: Mikrobiologiia. 64(1)

It is shown that secretion of bacteriolytic complex enzymes in a bacterium of the family Pseudomonadaceae begins in the latent and early logarithmic culture growth phases. A maximum of specific bacteriolytic activity falls in the same time interval w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7d8343b95e464fae2cfa2ecfdb9d079f
https://pubmed.ncbi.nlm.nih.gov/7715483

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[A lysoamidase bacteriolytic complex. 1. Determination of the nature of interaction of enzymes and the polysaccharide, included in the complex]

Autor: O A, Stepnaia, L A, Ledova, I S, Kulaev

Publikováno v: Biokhimiia (Moscow, Russia). 58(10)

The polysaccharide component of the bacteriolytic enzymatic complex "lysoamidase" (M(r) 1300 kDa) has been found to contain negatively charged ionic groups and can electrostatically interact with some enzymes within the complex. At pH 8.0 optimal for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6e8aa59f75d042c07fc027a74fe7d7f6
https://pubmed.ncbi.nlm.nih.gov/8268297

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[The components of the microbial preparation of lysoamidase from the Pseudomonodaceae family responsible for its bacteriolytic activity]

Autor: I S, Kulaev, A I, Severin, O A, Stepnaia, O V, Kruglaia

Publikováno v: Biokhimiia (Moscow, Russia). 54(2)

The contribution of enzymes isolated from the microbial enzymic preparation to its total bacteriolytic activity was studied. The combined action of the lytic proteinase L2 and the lytic fraction L1 used in the same ratio as in the lysoamidase prepara

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5f1d6b07686f8b923a49079827f1f125
https://pubmed.ncbi.nlm.nih.gov/2663084

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