I couldn't find one. This might be such an example:
Article What Makes a Protein Fold Amenable to Functional Innovation?...
I saw examples where the gene was cloned into a vector containing the His-tag N-terminal to the periplasmic export signal sequence, but the His tag would therefore not appear in the processed protein, and conventional chromatography was used for the purification.
Some journals claim that they will not accept kinetic data from enzymes containing tags and fusions, so there could be an issue with publication if you don't use the protein with the native sequence.