Displacement chromatography of proteins using a self-sharpening pH front formed by adsorbed buffering species as the displacer

Narahari, CR; Strong, JC; Frey, DD

HERO ID

5163292

Reference Type

Journal Article

Year

1998

Language

English

PMID

9842719

HERO ID 5163292
In Press No
Year 1998
Title Displacement chromatography of proteins using a self-sharpening pH front formed by adsorbed buffering species as the displacer
Authors Narahari, CR; Strong, JC; Frey, DD
Journal Journal of Chromatography A
Volume 825
Issue 2
Page Numbers 115-126
Abstract The preparative-scale separation of two proteins into adjoined, pure bands was accomplished using a novel, hybrid chromatography method which employs chromatofocusing using a self-sharpening pH front and displacement development. The method eliminates the use of a traditional displacer for accomplishing displacement chromatography, and was used to separate the A and B forms of beta-lactoglobulin using a strong-base anion-exchange column packing and a buffer system composed of acetic acid and either 3-(N-morpholino)propane-sulfonic acid (MOPS) or 2-(N-morpholino)ethanesulfonic acid (MES). Sample loads up to 150 mg of protein were applied to a 75 x 7.5 mm column to produce a displacement train composed of highly pure protein bands with greater than 90% recovery of protein. A discussion is given of the chromatographic behavior of proteins under concentration overloaded conditions for the case where a self-sharpening pH front formed using adsorbed buffering species is used to desorb proteins from an anion-exchange column packing.
Doi 10.1016/S0021-9673(98)00718-3
Pmid 9842719
Wosid WOS:000077119900002
Is Certified Translation No
Dupe Override No
Is Public Yes
Language Text English
Keyword displacement chromatography; preparative chromatography; chromatofocusing; mobile phase composition; proteins; lactoglobulins