From: Norman Watts (Norman_Watts$##$nih.gov)
Date: Thu May 01 2008 - 06:21:00 EDT
I'm not an organic chemist, but could use the advice of a chemist. I
want to label a Cysteine containing protein with mercury, but first I
am working with the Cysteine-minus mutant to determine the degree of
I am observing the binding of a variety of mercury compounds (e.g.
methyl mercury, PCMBS, merbromin) to the Cys-minus protein. The
occupancy is ~ 0.75 molar equivalents under a variety of conditions.
I have tried several agents, such as chelators, to remove this "non-
specifically" bound mercury. Cyanide ion is very effective in
removing much of the mercury, but there is a residual ~ 0.25 molar
equivalents that remains bound to the protein.
As I don't want to denature the protein (or, eventually, the Cysteine-
containing form) I need a mild means for removing the mercury. Can
anyone provide input on what groups in a protein, besides thiols,
might be reacting with organic mercury?
Norman Watts, Ph. D.
National Institutes of Health
50 South Drive, Rm. 1509
Bethesda, MD 20892-8025
Phone: (301) 402-3418
Fax: (301) 480-7629
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