12858_2017_84_MOESM2_ESM.pdf (220.63 kB)
Additional file 2: Figure S1. of Structural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase
journal contribution
posted on 2017-05-16, 05:00 authored by Gopinath Muruganandam, Arne Raasakka, Matti Myllykoski, Inari Kursula, Petri KursulaThe yeast PNK/CPDase and CPDase proteins purified by Ni-NTA affinity chromatography. A) SDS-PAGE from a Ni-NTA purification of ScTrl1 PNK/CPDase. M: marker, E1-E8: fractions eluted with 500 mM imidazole. The calculated size of the protein was 52.7 kDa. B) SDS-PAGE from Ni-NTA purifications of ScTrl1 CPDase and ScTrl1 (N+) CPDase. M: marker, SF1 and W1 are supernatant and wash flow-through samples from the purification of ScTrl1 CPDase, E1-E5: ScTrl1 CPDase fractions eluted with 500 mM imidazole. The calculated size of the protein was 32.2 kDa. SF2 and W2 are supernatant and wash flow-through samples from the purification of ScTrl1 (N+) CPDase, E6-E10: ScTrl1 (N+) CPDase fractions eluted with 500 mM imidazole. The calculated size of the protein was 32.4 kDa. C) SDS PAGE from a Ni-NTA purification of ScTrl1 (N-) CPDase. SF: supernatant flow-through, W: wash flow-through, E1-E10: fractions eluted with 500 mM imidazole, M: marker. The calculated size of the protein was 29.6 kDa. (PDF 220 kb)