Bonded-phase selection in the high-performance liquid chromatography of proteins
| Autor: | Richard Ludwig, Lloyd A. Witting, Daryl J. Gisch, Roy Eksteen |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
Chromatography
Chemistry Hydrophilic interaction chromatography Organic Chemistry Ion chromatography General Medicine Reversed-phase chromatography Biochemistry Displacement chromatography High-performance liquid chromatography Analytical Chemistry Column chromatography Supercritical fluid chromatography Thermoresponsive polymers in chromatography |
| Zdroj: | Journal of Chromatography A. 296:97-105 |
| ISSN: | 0021-9673 |
| DOI: | 10.1016/s0021-9673(01)96403-9 |
| Popis: | The importance of several parameters in the reversed-phase high-performance liquid chromatography of proteins was investigated. Branching of the bonded phase, as in neohexyl versus n- hexyl, was found to be beneficial in reducing interaction of residual surface silanols with small basic analytes, but detracted from the chromatography of proteins. A deactivation procedure which reduced deleterious interaction of small, basic analytes with the packing also improved the chromatography of proteins. Varying the bonded-phase chain length from octyl to hexyl and then to butyl had relatively little effect on peak shape and recovery. Shortening the bonded-phase chain length, however, did decrease protein retention, particularly for proteins with molecular weights of 35,000 and 77,000 daltons. Increasing silica pore size from 12 nm to 30 nm appeared to improve the chromatography of proteins. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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