Gel-Filtration Chromatography

Abstract

Gel-filtration chromatography is a popular and versatile technique that permits the effective separation of proteins and other biological molecules in high yield. Here, the basis of the method is described and typical matrix types are contrasted. The selection of suitable operating conditions and applications of the method are also discussed.

Molecular cloning, expression and purification of lactoferrin from Tibetan sheep mammary gland using a yeast expression system

“…Ion-272 exchange chromatography has several advantages over affinity 273 chromatography, and it was once a common method for the puri-274 fication of LF [28,29]. Gel-filtration chromatography is a popular 275 and versatile method that effectively separates proteins, at high 276 yields [30]. Thus, to extract rLF with high purity for possible use 277 in subsequent industrial manufacture, we chose gel-filtration chro-278 matography for the last step in the three-step purification protocol.…”

Shotgun EM of mycobacterial protein complexes during stationary phase stress

“…So far, size exclusion chromatography has been the most popular fractionation method ( Maco et al., 2011 ; Kastritis et al., 2017 ; Verbeke et al., 2018 ) with selection of high MW fractions because larger proteins are easier to reconstruct by TEM. For the same reason, we imposed a MW cut-off at 100 kDa, but applied anion chromatography to bind proteins and enrich for rare complexes ( Ó’Fágáin et al., 2011 ) ( Fig. 1 c and d).…”

Expression, Purification, and Characteristic of Tibetan Sheep Breast Lysozyme Using <italic>Pichia pastoris</italic> Expression System

“…The best elution condition was with a buffer of 0.25 M sodium chloride and 50 mM Tris buffer at a pH of 9.0. Gel-filtration chromatography is a popular and versatile method that pursued the effective separation of proteins and high yield ( Ó’Fágáin et al, 2011 ). In order to obtain high purity rSLZ and apply in possible subsequent industrial manufacture, gel-filtration chromatography was selected for the last step to purify rSLZ.…”