Fig. 1: L-Asp transport rates catalyzed by purified and reconstituted GltTk as a function of the concentrations of Na+ and L-aspartate.
From: Kinetic mechanism of Na+-coupled aspartate transport catalyzed by GltTk

The rates represent the combined contributions of right-side-out and inside-out oriented proteins. a Aspartate-dependent measurements at different fixed Na+ concentrations. The lines represent fits of the Michaelis-Menten equation to the data for uptake at Na+ concentrations of 5āmM (red), 10āmM (orange), 25āmM (yellow), 50āmM (green), 100āmM (cyan), 200āmM (blue), 300āmM (purple). b Sodium-dependence of transport at fixed L-Asp concentrations. The lines represent fits of the Hill equation to the data for uptake at 0.05āµM (red), 0.1āµM (orange), 0.5āµM (yellow), 1āµM (green), 5āµM (cyan), 10āµM (light blue), 50āµM (blue), 100āµM (purple). Each uptake rate represents the average of three independent biological replicates, each constituted by two technical replicates, and the standard error of the mean is shown.