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pH‐Regulated electroretention chromatography: Towards a new method for the separation of proteins according to their isoelectric points
Author(s) -
Korlach Jonas,
Hagedorn Rolf,
Fuhr Günter
Publication year - 1998
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150190713
Subject(s) - isoelectric focusing , isoelectric point , chromatography , chemistry , fractionation , fiber , cytochrome c , protein purification , field flow fractionation , biochemistry , enzyme , organic chemistry , mitochondrion
The pH‐dependent electroretention behavior of model proteins cytochrome c and ribonuclease A was studied in a hollow fiber arrangement, similar to that used in electrical field‐flow fractionation. Field‐induced immobilization of the proteins at the inner wall of the fiber was a function of the pH adjusted in the solution surrounding it, indicating that the pH inside the fiber lumen, relevant for protein migration, quickly equilibrates to the regulated value outside. A complete separation of the model proteins was achieved. Advantages of the principle as well as prospects for the development of a technique separating more than two protein species according to their isoelectric points are discussed.