Production of the recombinant antimicrobial peptide UBI18-35 in Escherichia coli; Protein Expression and Purification; Vol. 143

Bibliografske podrobnosti
Parent link:Protein Expression and Purification
Vol. 143.— 2018.— [P. 38-44]
Korporativna značnica: Национальный исследовательский Томский политехнический университет Исследовательская школа химических и биомедицинских технологий
Drugi avtorji: Ashcheulova D. O., Efimova L. V. Lina Viktorovna, Lushchyk A. Y., Yantsevich A. V., Baykov A. N. Aleksandr Nikolaevich, Pershina A. G. Aleksandra Gennadievna
Izvleček:Title screen
Radiolabeled peptides derived from ubiquicidine (UBI) are of great interest for early and highly accurate scintigraphic detection and differentiation of infection and sterile inflammation. In the present work the recombinant antimicrobial peptide UBI18-35 - a fragment of the human natural cationic peptide ubiquicidine - was produced in Escherichia coli for the first time. The insoluble expression of the peptide in fusion with ketosteroid isomerase provided high yield, about 6 mg of UBI18-35 per liter. We developed an approach to produce the antimicrobial peptide UBI18-35, that encompasses inclusion body isolation and size exclusion chromatography. This method could be the basis for industrial biotechnological production of diagnostic system components that are in high demand.
Jezik:angleščina
Izdano: 2018
Teme:
Online dostop:https://doi.org/10.1016/j.pep.2017.10.011
Format: Elektronski Book Chapter
KOHA link:https://koha.lib.tpu.ru/cgi-bin/koha/opac-detail.pl?biblionumber=667254

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200 1 |a Production of the recombinant antimicrobial peptide UBI18-35 in Escherichia coli  |f D. O. Ashcheulova, L. V. Efimova, A. Y. Lushchyk [et. al] 
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330 |a Radiolabeled peptides derived from ubiquicidine (UBI) are of great interest for early and highly accurate scintigraphic detection and differentiation of infection and sterile inflammation. In the present work the recombinant antimicrobial peptide UBI18-35 - a fragment of the human natural cationic peptide ubiquicidine - was produced in Escherichia coli for the first time. The insoluble expression of the peptide in fusion with ketosteroid isomerase provided high yield, about 6 mg of UBI18-35 per liter. We developed an approach to produce the antimicrobial peptide UBI18-35, that encompasses inclusion body isolation and size exclusion chromatography. This method could be the basis for industrial biotechnological production of diagnostic system components that are in high demand. 
461 |t Protein Expression and Purification 
463 |t Vol. 143  |v [P. 38-44]  |d 2018 
610 1 |a труды учёных ТПУ 
610 1 |a электронный ресурс 
610 1 |a antimicrobial peptides 
610 1 |a ubiquicidine 
610 1 |a ketosteroid isomerase 
610 1 |a size exclusion chromatography 
610 1 |a Inclusion bodies 
610 1 |a компоненты 
610 1 |a антимикробные пептиды 
610 1 |a диагностические системы 
610 1 |a эксклюзионная хроматография 
701 1 |a Ashcheulova  |b D. O. 
701 1 |a Efimova  |b L. V.  |g Lina Viktorovna 
701 1 |a Lushchyk  |b A. Y. 
701 1 |a Yantsevich  |b A. V. 
701 1 |a Baykov  |b A. N.  |g Aleksandr Nikolaevich 
701 1 |a Pershina  |b A. G.  |c biologist  |c Associate Professor of Tomsk Polytechnic University, Candidate of biological sciences  |f 1981-  |g Aleksandra Gennadievna  |3 (RuTPU)RU\TPU\pers\32466  |9 16414 
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