Two students were playing around with a computer simulation of protein
purification. They had a protein with a Pi of 8.1, wich was a single
band on 2D-electroforesis. However, at pH 7.5 the protein was bound both
to an anion and a cation exchange matrix.
Can anyone explain how this is possible and if it could occur in real
life? I doubt that the program simulates nonspecific binding to the
matrix?
(Sorry about the slightly vague details, I have not seen their results
myself yet).
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Kaj Stenberg, Ph. D
Department of Biosciences tel. +358-9-191 59682
Division of Biochemistry fax +358-9-191 59068
P. O. Box 56, Viikinkaari 5 e-mail: kaj.stenberg at helsinki.fi
FIN-00014 University of Helsinki http://www.helsinki.fi/~kstenber/
Finland
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