Purification of plasmid (pVaxLacZ) by hydrophobic interaction chromatography

Moreira, Keila Aparecida; Diogo, Maria Margarida; Prazeres, Duarte Miguel F.; Filho, José Luiz de Lima; Porto, Ana Lúcia Figueiredo

doi:10.1590/s1516-89132005000400014

Cited by 9 publications

(2 citation statements)

References 7 publications

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“…Some chromatographic techniques have been used to purify pDNA, such as anion-exchange chromatography (AEC) (Hines et al, 1992;Prazeres et al, 1998;Franc et al, 2010), size-exclusion chromatography (SEC) (Horn et al, 1995), hydrophobic-interaction chromatography (HIC) (Gurunathan et al, 2000;Diogo et al, 2003;Duarte et al, 2004;Moreira et al, 2005;Pereira et al, 2010) and affinity chromatography (AC) (Wils et al, 1997;Sandberg et al, 2004). These chromatographic methods work well in removing host contaminants (protein, RNA, endotoxins, genomic DNA, etc.…”

Section: Research Articlementioning

confidence: 99%

Using a single hydrophobic-interaction chromatography to purify pharmaceutical-grade supercoiled plasmid DNA from other isoforms

Bo¹,

Wang²,

Chen³

et al. 2012

Pharmaceutical Biology

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Section: Research Articlementioning

confidence: 99%

Using a single hydrophobic-interaction chromatography to purify pharmaceutical-grade supercoiled plasmid DNA from other isoforms

Bo¹,

Wang²,

Chen³

et al. 2012

Pharmaceutical Biology

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“… 13 Critical quality attributes of ADCs that have successfully been analyzed, include the average drug‐to‐antibody ratio, 14 and drug‐load distribution. 15 Recently, new applicability areas have been explored, including the HIC purification of viruses, 16 and the analysis of plasmids 17 and exosomes. 18 …”

Section: Introduction To Hydrophobic Interaction Chromatographymentioning

confidence: 99%

A protocol for setting‐up robust hydrophobic interaction chromatography targeting the analysis of intact proteins and monoclonal antibodies

Ewonde

Lingg

Eßer

et al. 2022

Analytical Science Advances

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Hydrophobic interaction chromatography (HIC) is a chromatographic technique that mainly targets the separation of biomolecules (intact proteins, monoclonal antibodies, etc.) based on the difference in surface hydrophobicity while applying non-denaturing conditions. This protocol paper provides guidelines for setting-up robust HIC analysis and considers the instrument configuration, mobile-phase and sample preparation, as well as chromatographic conditions and settings. The separation of a mixture of intact proteins and monoclonal antibodies is demonstrated by applying conventional HIC conditions, that is, using a mildly hydrophobic (C 4 ) stationary phase in combination with an inverse ammonium sulphate gradient dissolved in aqueous phosphate buffer. The effect of sample-preparation conditions on sample breakthroughs is presented. Finally, good run-to-run repeatability (relative standard deviation < 2%) is demonstrated for five different columns obtained from three different column lots, considering chromatographic retention, peak width, peak area and column pressure.

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