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detection of protein phosphorylation using M.S.


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#1 flin

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Posted 25 March 2005 - 09:01 PM

Is it possible to detect protein phosphorylation by mass spec using lysate? If the sample has to be enriched before M.S., what will be the best way to do it?

#2 leekaming

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Posted 26 March 2005 - 08:14 AM

Mass spectrometry should be able to identify the difference in MW of phosphorylated and unphosphorylated protein. MALDI-TOF should be able to distinguish difference of 10Da!

#3 flin

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Posted 26 March 2005 - 01:43 PM

Thanks for the info!
I guess my question is what if I don't know what I am looking at or I want to look at all the molecules along a signaling pathway. Can I load samples from a mixture of many different proteins (after digestion) to m.s. and identify their phosphorylation state? If so, it would be a lot more efficient than other methods like WB, FACS and microarray.

#4 fred_33

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Posted 29 March 2005 - 12:30 AM

hi
i've done phosphorylation state analysis once, and for analyzing particular protein, i suppose it's better to separate them on gel and after input one by one in the MS. That is what we did...

#5 flin

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Posted 29 March 2005 - 10:49 PM

Thx!


hi
i've done phosphorylation state analysis once, and for analyzing particular protein, i suppose it's better to separate them on gel and after input one by one in the MS. That is what we did...

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