. 2013 Oct 9;4:2529. doi: 10.1038/ncomms3529

Table 1. Apparent K _m and V _max values for each substrate.

	APP		Notch		APLP2
	C83	C99	V1711	ΔE	R678	M664
K_m (K_app), nM	449.9±95.2	784.6±123.4	550.3±114.3	1,337.0±85.3	388.8±88.3	431.6±65.3
V_max, pM min⁻¹	365.9±93.0	134.0±22.9	431.7±30.4	217.2±19.8	342.2±45.4	83.6±16.4
V_max/K_m	0.81±0.10	0.17±0.04	0.84±0.13	0.17±0.03	0.88±0.04	0.19±0.04

Defined amount of each substrate was incubated with γ-secretase fraction for 4 h. Protein samples were subjected to western blotting with AICD–FLAG being the authentic standards. ICD produced from each substrate was visualized with anti-M2 FLAG antibody, and their intensities were quantified (see Fig. 2). V_max/K_m values, which indicate catalytic efficiency of γ-secretase, were roughly fivefold greater for substrates containing a short ectodomain compared with those with a long ectodomain. Data are expressed as means±s.d. of three independent experiments.

Table 1. Apparent K m and V max values for each substrate.

Table 1. Apparent K _m and V _max values for each substrate.