during purification of ubiquitin and ubiquitin with an H68A mutation, you observe that the elutionz from the sulfopropyl (S) cation exchange columns at pH 4.5 are distinct. however your lab "helper" didnt label which sample was which. based on your knowledge of protein purification, which one of the proteins would elute first from the S column during an elution by increasing salt concentration? NOTE: H68A means that the histidine at position 68 has been replaced with an alanine in that protein. in this instance it is a single amino acid difference and only changes the side chain
Added by Gregory H.
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5, a sulfopropyl (S) cation exchange column binds positively charged proteins. The binding strength depends on the net positive charge of the protein; more positive charge means tighter binding and later elution with increasing salt. Show more…
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