metall ion affinity purification of proteins - something better

Dr. Hiranya S. Roychowdhury hroychow at
Sun Jul 2 20:16:38 EST 2000

The affinity purification of a protein would certainly depend on the
available antibody or antigen or the metal affinity (in case of 6xH). The
one quite widely used system is the glutatione-S-transferase fusions. The
fusion protein is purified by taking advantage of the glutathione-binding
of GST.
Other than these usual fusion protein affininity purifications, there may
be avenues that take advantage of the properties of the proteins being
purified, eg. affinity of the protein to nucleotides (use of cibacron blue
column); if post-transl. modification happens, conjugated/modified proteins
(eg., glycoproteins) may be piurified with the use of a ligand like ConA....
The possibilities really depend on the protein itself.

Did this help? Or did I not grasp the query properly?

At 10:46 PM 7/2/00 +0100, Wolfgang Schechinger wrote:
>Hi all, 
>are there other (competitive/better) methods for purifying proteins 
>using affinity to chelated metal ions than his6 / nickel?
>all input is welcome!
>This message is encrypted. Use your brain to decode it.
>Dr. Wolfgang Schechinger, Dept. of Pathobiochemistry
>University of Tuebingen, Germany
>email: wolfgang.schechinger at 
>usual disclaimers apply 
Dr. Hiranya Sankar Roychowdhury
Dept. of Molecular Biology	
PO Box 30001 - 3MLS
New Mexico State University
Las Cruces, NM 88003

Lab: (505) 646 4722
Office: (505) 646 8256
hroychow at


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