Related Experiment Video
Updated: Oct 2, 2026

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method
Published on: July 27, 2016
[Comparative analysis of gamma globulin preparations isolated by means of DEAE-Sephadex and DEAE-cellulose]
Abstract:
Preparations of rabbit gamma-globulin obtained with the aid of ion-exchange chromatography on DEAE-Sephadex contained an admixture of other serum proteins revealed by disc-electrophoresis in acrylamide gel. This impurity can be eliminated by rechromatography of gamma-globulin preparations of DEAE-cellulose in the same buffer solutions which were used for purification of gamma-globulin on DEAE-Sephadex. Better purification of gamma-globulin on DEAE-cellulose can supposedly be attributed to the effective absorption on cellulose basis of euglobulin aggregates which form in the solutions with a low ionic power used for chromatographic isolation of gamma-globulin on ion-exchangers.
More Related Videos
Related Concept Videos
SDS-PAGE
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
Two-dimensional Gel Electrophoresis
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as cells...
Types Of Column Chromatography
Gel Filtration Chromatography
When the...
Capillary Electrophoresis: Applications
Capillary zone electrophoresis (CZE) separates ionic components based on their electrophoretic mobility. It has been used to separate proteins, amino acids,...

