Hi,
I have narrowed down two possible mechanisms for my favorite protein. One mechanism involves a charged intermediate (which I can trap) and the other uncharged intermediate. - Does anyone have any idea for experiments to distinghuish between a +1 and neutral - the enzymes size is 35kDa
Thank you.
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#2
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Enthusiast
Posted 27 October 2011 - 01:39 PM
Would native PAGE be an option? Unlike SDS-PAGE, native separates by size and charge
#3
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an elder
Posted 28 October 2011 - 07:45 AM
urea-page should work. urea enhances charge separation. we used to determine the phosphorylation state of a protein with this method.
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