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Národní úložiště šedé literatury Nalezeno 2 záznamů.  Hledání trvalo 0.00 vteřin. 
Expression of osmotin, an antifungal protein from Nicotiana tabacum in Escherichia coli
 Viktorová, J. ; Macková, M. ; Macek, Tomáš
Plants have evolved a huge variety of proteins involved in the defense against pathogens and adaptation to stressful environments. Plant proteins whose expression is strongly induced in response to infection by pathogens belong to the group of pathogenesis-related (PR) proteins. The family of PR-5 proteins constitutes a group of cysteine-rich proteins including thaumatin, zeamatin and also osmotin. Osmotin is a cationic protein of 205 residues and molecular weight of 24 kDa. It was discovered and characterized in cells of Nicotiana tabacum var. Wisconsin 38. The plasmid harbouring cDNA of osmotin from Nicotiana tabacum was constructed for transformation of Escherichia coli. The osmotin gene was prepared in fusion with histidine tail to facilitate the isolation and purification from bacterial cells. Selection of transgenic colonies was based on antibiotic resistance. The hexahistidine-tagged osmotin was overexpressed in heterologous system by using pET expression vector and purified using immobilized metal affinity chromatography. The expression of osmotin was detected and antifungal activity was tested.
Úplný záznam
Isolation and study of the properties of recombinant pseudoosmotin
 Richterová, K. ; Nováková, Martina ; Antošová, Z. ; Neubauerová, Tereza ; Macková, Martina
Antimicrobial peptides represent new clinical compounds with antimicrobial action and they could participate in solving the problem of ever-increasing resistance of microorganisms to the traditional antibiotics. The aim of this work was to study optimal conditions for expression, isolation and purification of recombinant pseudoosmotin from Escherichia coli BL21 (DE3). Pseudoosmotin was isolated from membrane fraction of bacteria and was purified by the affinity chromatography using Ni-NTA. Isolated pseudoosmotin did not show antimicrobial activity against studied microorganisms.
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