. 2022 Mar 18;298(5):101848. doi: 10.1016/j.jbc.2022.101848

Table 1.

Kinetic parameters for αSN glycation^a

Binding mode	Glycating agent	K_D (mM)^b	k_max (h⁻¹)^b	Initial slope (h⁻¹M⁻¹)^c
Saturation binding	MGO	15.8 ± 6.12	37.8 ± 4.98	2392
Saturation binding	Ribose	486 ± 188	36.8 ± 4.41	75
Linear^c	Mannose	-	-	3.91 ± 0.26
	Glucose	-	-	3.43 ± 0.00
	Galactose	-	-	3.10 ± 0.01
	Lactose	-	-	2.81 ± 0.16
	Fructose	-	-	1.19 ± 0.13
	Sucrose	-	-	No detectable signal

All data based on fluorescence time profiles normalized by the extent of modification (see main text).

The rate constant for glycation k_obs was obtained from exponential decays in Figure 1, B and C. Plots of k_obsversus glycating agent concentration were then fitted to a Michaelis–Menten type model to obtain the apparent affinity of the agent for αSN (K_D) and the maximal velocity at high agent concentrations (k_max).

Initial velocities at every glycating agent concentration was obtained from normalized slopes versus time at time t = 0. The table provides the slope obtained from plotting initial velocities versus glycating agent concentration (in the case of MGO and ribose, whose glycation profile followed an exponential decay, the slope was obtained as the tangent at zero concentration).