It is usually mentioned "Phosphate Buffer" in references but I am trying to figure out as to which of these two (Sodium or Potassium) Phosphate Buffers would be appropriate for the purification of especially Myosin proteins.
Is there any significant difference or they can be used alternatively?
If you want to use Potassium Phosphate for protein purification you should separate your purified proteins with PAGE but using an another detergent instead SDS due to insoluble potassium salt of SDS which also precipitate your proteins in the gel.
I think the main difference is in the solvation sphere of either Na or K. For most proteins, it probably won't have a significant difference, but some proteins may be more stable with one ion over another. For instance, one of the proteins I was studying would precipitate when in NaCl, but was stable in KCl.
Erman Kocak Thank you for your comments, If I could ask another adding question pertaining to your reply then do you know any other detergent that replaces SDS? Or is Native Page a better option in that case?
And as per Stephen Boulton & Ali Mahmoudpour I think its best if I compare the results for either of them. Thank you!
I think SDS-PAGE is inevitable in case of protein purification at least for the screening of purity of the samples that‘s why I would suggest you to use another buffer except potassium phosphate. Of course you can separate your samples with other electrophoresis methods which is not as routinized as SDS-PAGE for example with a cationic detergent;16-BAC based electrophoresis, but you should consider the preparation of 16-BAC gel that differs totally from SDS-Gels
Ali Mahmoudpour that is a really helpful piece of information. Thank you
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