Provided that the cultured cells were supplemented with sufficient metal salts during their growth phase
Some metalloproteins bind metal ions relatively weakly, so may be isolated in the apo form (i.e., no metal bound), depending on the method. In such cases, the metal can be included in the buffer during purification, which may improve stability, or later when measuring activity of the protein. An example is methionine aminopeptidase.
If there is EDTA present in the buffer during purification, nonstructural metal ions may be stripped out of the protein. It may be preferable not to include a metal chelator in such cases.
Dear Aria Mcullum
I'm agree with Adam B Shapiro
since in general the affinity of metalloproteins is in micro molar range is it possible that at the end of purification process, you will obtain an apo or partially metallated form, expecially if you are using for purification approaches as IMAC where there are also different metals that can interfeere.
I suggest to you to produce apo form by incubating the protein with EDTA, remove the EDTA by desalting and add again the metal.
you can use DSF and check how the tm change under metal addition to check if the protein bind the metal..
in the following paper you can find an example of this on the following paper
https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0081306
good luck
Manuele
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