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Can gel filtration effect buffer composition? - (May/05/2008 )

I am currently trying to purify a solubilized receptor using gel filtration. To test for the presence of my solubilized receptor in solution i apply it to a receptor binding assay (RBA) and when it is present it reduces binding of my fusion protein ( heat insensitive AP fusion protein) to my membrane, which i pellett and test using p-npp (an ap detection substrate, amount of AP determined using a spectrometer, more absorbance = more fusion protein bound). I compare normal binding of the fusion protein to binding when a solubilized receptor is present. Binding is decreased (absorbance less) when solubilized receptor is present.

Interestingly after gel filtration and concentration of my sample, when I apply fractions obtained from the column to my RBA (100 ul into 500ul) I get greater then normal binding (higher absorbance). I dont understand this as my column buffer is the same as the buffer i use to solubilize my membrane in (HBSS) and when i add HBSS alone there is no effect to binding. Could filtration of my buffer in a 45 micron filter or sterilization of the column buffer alter its actions in my RBA? Or is the filtration column altering my buffer composotion? Any help would be appriciated.

J

-jturne5-

QUOTE (jturne5 @ May 6 2008, 09:20 AM)
I am currently trying to purify a solubilized receptor using gel filtration. To test for the presence of my solubilized receptor in solution i apply it to a receptor binding assay (RBA) and when it is present it reduces binding of my fusion protein ( heat insensitive AP fusion protein) to my membrane, which i pellett and test using p-npp (an ap detection substrate, amount of AP determined using a spectrometer, more absorbance = more fusion protein bound). I compare normal binding of the fusion protein to binding when a solubilized receptor is present. Binding is decreased (absorbance less) when solubilized receptor is present.

Interestingly after gel filtration and concentration of my sample, when I apply fractions obtained from the column to my RBA (100 ul into 500ul) I get greater then normal binding (higher absorbance). I dont understand this as my column buffer is the same as the buffer i use to solubilize my membrane in (HBSS) and when i add HBSS alone there is no effect to binding. Could filtration of my buffer in a 45 micron filter or sterilization of the column buffer alter its actions in my RBA? Or is the filtration column altering my buffer composotion? Any help would be appriciated.

J

Off the top of my head, I'd say you might have removed some inhibitors.

-swanny-

Did you have the same detergent concentration in samples and elution buffers?

-genehunter-1-

Swanny is probably right.

-rosewater-

yes i think that is the problem. I have done a trial run "ballparking" the detergent concentration of my previous sample, and my results improved, it also increased the liability of the receptor. I will be sure to make the detergent concentration in the elution buffer the same as the concentration in the samples. THANKS!

J

-jturne5-