Publications by authors named "Ronni G Hansen"
Article Synopsis
- - The study compared various cation-exchange resins, such as Fractogel and MacroPrep, in terms of several chromatographic factors like pH dependence, efficiency, and particle size, specifically analyzing their performance with proteins like Anti-FVII Mab, aprotinin, and lysozyme.
- - It was found that for proteins with a pI above the experimental pH, pH had little impact on retention, whereas the Anti-FVII Mab showed binding at pH 7.5 on multiple resins, and increased flow rates led to higher plate height in efficiency measurements.
- - The research also highlighted the significant influence of salt concentration on binding strength and revealed that competitive binding from fermentation components lowered the dynamic binding
Article Synopsis
- A comparative study examined various chromatographic resins, including heparin and cation exchangers, analyzing factors like efficiency, binding strength, and capacity.
- The experiments involved four different proteins, showing that pH had a minimal effect on retention for proteins with high isoelectric points, but certain resins had a notable decrease in retention as pH rose.
- Results indicated that cation-exchange resins’ binding strength varied with ionic strength and protein type, with significant dynamic capacity utilized during operations, revealing potential substitutes for heparin resins in specific conditions.*
A comparative study was performed on strong cation-exchangers to investigate the pH dependence, efficiency, binding strength, particle size distribution, static and dynamic capacity, and SEM pictures of chromatographic resins. The resins tested included: SP Sepharose XL, Poros 50 HS, Toyopearl SP 550c, SP Sepharose BB, Source 30S, TSKGel SP-5PW-HR20, and Toyopearl SP 650c. Testing was performed with four different proteins: anti-FVII Mab (IgG), aprotinin, lysozyme, and myoglobin.
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