Packings and stationary phases for biopolymer separations by HPLC |
| |
Authors: | K K Unger R Janzen G Jilge |
| |
Institution: | 1. Institut für Anorganische Chemie und Analytische Chemie, Johannes Gutenberg-Universit?t, D-6500, Mainz, FRG
|
| |
Abstract: | Summary Packings and stationary phases applied to high resolution separations of proteins, enzymes, and nucleic acids must satisfy
a series of distinct criteria that are different from those usually required by HPLC of low molecular weight non-biologically
active analytes. These requirements have been met through substantial improvements in classical gel media together with novel
developments in silica supports, and have led to a family of products with tailor-made and reproducible properties. Supports
consisting of cross-linked organic gels, and inorganic materials (mostly silicas) are now available with graduated particle
sizes, pore sizes, porosities and surface areas as well as non-porous beads. A whole range of stationary phases, such as reversed
phase, hydrophobic interaction, ion exchanger and affinity packings, were designed for application as chemical sensors for
biopolymer recognition in adsorptive chromatography. The phase systems are operated in the gradient mode, giving high resolution
and high peak capacities. In addition, aqueous liquid-liquid partitioning systems have been developed for the fractionation
of proteins and nucleic acids. Size exclusion media complete the set of HPLC variants enabling a discrimination of proteins
according to their size and shape in an isocratic elution mode. Basically, protein purification and isolation is a multistage
process where-by the HPLC variants are combined in a logistic sequence, utilizing the different selectivities of the phase
systems and thus maximising resolution, speed and throughput. |
| |
Keywords: | Column liquid chromatography Biopolymer separation Stationary phases and packings Properties Stationary/mobile phase combination and selection |
本文献已被 SpringerLink 等数据库收录! |
|