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Urh Černigoj

Researcher at BIA Separations (Slovenia)

Publications -  25
Citations -  335

Urh Černigoj is an academic researcher from BIA Separations (Slovenia). The author has contributed to research in topics: Affinity chromatography & Elution. The author has an hindex of 9, co-authored 25 publications receiving 267 citations.

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Journal ArticleDOI

Towards automation in protein digestion: Development of a monolithic trypsin immobilized reactor for highly efficient on-line digestion and analysis

TL;DR: Novel trypsin-based monolithic immobilized enzyme reactors, obtained by covalent immobilization on convective interaction media (CIMac™) analytical columns, showed high sensitivity down to the pmole level and were suitable for the analysis of high-molecular weight proteins.
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A multimodal histamine ligand for chromatographic purification of plasmid DNA.

TL;DR: A novel monolithic chromatographic support bearing multimodal histamine (HISA) groups was developed and characterized, enabling separation of supercoiled (sc) pDNA from other plasmid isoforms (and other process related impurities) by adjusting salt or pH gradient.
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Histamine monolith versatility to purify supercoiled plasmid deoxyribonucleic acid from Escherichia coli lysate.

TL;DR: In this article, the physicochemical properties of histamine ligand in a supercoiled plasmid DNA purification process from an Escherichia coli clarified lysate, where the emphasis is given to the elution strategy that allows higher selectivity and efficient removal of other impurities besides the open circular isoform.
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Characterization of methacrylate chromatographic monoliths bearing affinity ligands.

TL;DR: IgGs toward different plasma proteins were immobilized via the hydrazide coupling chemistry to provide oriented immobilization and DBC was found to be flow independent and was increasing with the size of bound protein.
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Titanium dioxide nanoparticle coating of polymethacrylate-based chromatographic monoliths for phosphopetides enrichment.

TL;DR: The first synthesis and characterization of immobilisation of rutile TiO2 nanoparticles onto organic monolithic chromatographic support (CIM-OH-TiO2) is reported, opening the possibility for a faster, more selective enrichment of phosphopeptides from biological samples that will enable future advances in studying protein phosphorylation.