Dimerization of Glutathione-S-Transferase

Cornelius Krasel krasel at wpxx02.toxi.uni-wuerzburg.de
Sun Jul 14 15:52:24 EST 1996


Dima Klenchin (klenchin at facstaff.wisc.edu) wrote:
> In article <12JUL199617473807 at watson.bms.com>, curtis at watson.bms.com (Michael S Curtis) wrote:
> #Does anyone know if glutathione-s-tranferase dimerizes giving a molwt of 
> #approx 59,000? If anyone has any info please post.
> 
> Yes, it does. But if you mean on gels, don't be confused: on SDS gel it 
> always runs as a single band. 

In my experience, I've also seen dimerization and aggregation of GST
on SDS gels. It appears that GST can become crosslinked by disulfide
bonds since reducing agents partially reverse dimerization.

Actually the dimerization properties of GST have been used recently
to study dimerization of some <whatever> subunits expressed as GST
fusion proteins (one of the latest JBCs).

--Cornelius.

-- 
/* Cornelius Krasel, U Wuerzburg, Dept. of Pharmacology, Versbacher Str. 9 */
/* D-97078 Wuerzburg, Germany   email: phak004 at rzbox.uni-wuerzburg.de  SP3 */
/* "Science is the game we play with God to find out what His rules are."  */



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