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. 2023 Nov 29;15(12):2344. doi: 10.3390/v15122344

Figure 7.

Figure 7

N-terminal sequencing of a purified processed Pol*-His fragment. Prot-Pol*-His was purified via IMAC and subjected to SDS-PAGE. The Coomassie stained gel showed the unprocessed Prot-Pol*-His (60 kDa) and the cleaved Pol*-His fragment (28 kDa). After blotting onto a PVDF membrane and staining, the Pol*-His fragment was excised and analyzed via Edmann degradation. The small amount of protein in the 28 kDa band led to an early termination of the sequencing reaction, and only the first three degradation steps yielded clear results. Since the sequence of the expression construct was known, the amino acid sequence serine (step 1), proline (step 2), and serine (step 3) could nevertheless be assigned to cleavage at position P1′ S2394.