Peptides and proteins were separated by reversed-phase chromatography on a 30 x 4.6 mm I.D. column packed with non-porous crosslinked polystyrene particles having a mean particle diameter of 3 micron and a rugulose surface. The polymeric support did swell slightly in organic solvents, but the estima
Micropellicular stationary phases for rapid protein analysis by high-performance liquid chromatography
β Scribed by Krishna Kalghatgi
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 915 KB
- Volume
- 499
- Category
- Article
- ISSN
- 1873-3778
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β¦ Synopsis
The high separating speed, efficiency and operational stability of various micropellicular stationary phases are demonstrated in the high-performance liquid chromatography (HPLC) of biopolymers. The micropellicular sorbents were prepared from 2-microns fluid-impervious silica microspheres as the support, with a thin layer of different retentive materials at the surface. These include a molecular fur of octyl or stearyl chains for reversed-phase chromatography as well as a hydrophilic layer with amino groups and polyethyleneglycol chains for anion-exchange and hydrophobic interaction chromatography, respectively. The use of appropriate micropellicular stationary phases for protein separation by metal-interaction and affinity chromatography is also illustrated. In most cases, operation at elevated column temperature was found to be preferable for rapid separations. Preliminary results show that the stability of micropellicular columns compares very favorably with that of columns conventionally used in HPLC and that they are easy to maintain.
π SIMILAR VOLUMES
A new procedure using high-performance liquid chromatography for the rapid separation of cellulase proteins is described. The cellulase components of Trichoderma reesei are fractionated on a DEAE anion-exchange column using a phosphate buffer at pH 6.2. Activities of the individual components obtain