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Additional file 2: Figure S1. of Structural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase

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posted on 16.05.2017, 05:00 by Gopinath Muruganandam, Arne Raasakka, Matti Myllykoski, Inari Kursula, Petri Kursula
The 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)

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Forschungs- und Wissenschaftsstiftung Hamburg (DE)

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