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. 2018 Jan 2;9:38. doi: 10.1038/s41467-017-02444-w

Fig. 3.

Fig. 3

Mutations in GltPh alter the substrate selectivity to prefer neutral amino acids L-[3H]aspartate (100 nM; green triangles), L-[3H]serine (1 µM; red circles), L-[3H]alanine (1 µM; blue squares) and L-[3H]glutamine (1 µM; purple diamonds) transport by wild-type GltPh a, GltPh-R397C c and GltPh-G396S/R397C e in the presence of an inwardly directed Na+ gradient at pH 7.5. Uptake of each substrate in the absence of a Na+ gradient is shown in open, black symbols, of which multiple are overlayed. b L-[3H]aspartate concentration–response for wild-type GltPh. L-[3H]serine (red circles) and L-[3H]alanine (blue squares) concentration responses are shown for GltPh-R397C d and GltPh-G396S/R397C f. Values presented are mean ± S.E.M, (n ≥ 3)