I'm trying to swap the Zn2+ in an enzyme with other divalent
cations, but everytime I do it, the protein precipitates. I
more or less dialyze the protein in 50mM Tris-HCL, pH 7.4,
with 1-10 mM of the cation2+; the protein is stable in
the Tris by itself. Does anyone know of a way to stablize the
transition? One caveat: the enzyme is quite concentrated
(2.1 mg/ml), and I have thought of diluting it a bit. But I
will have to reconcentrate it to 12 mg/ml, so this does not
seem to solve the problem.
Any ideas would be appreciated.
-Dirk
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Dirk Bussiere bussierd at tvsfrank.pprd.abbott.com
Abbott Laboratories Office: (847)935-0916
Department 42T FAX: (847)937-2625
100 Abbott Park Rd.
Abbott Park, IL 60064-3500
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