Table 1.

Glycosylation of sAPPα and sAPPβ in brain extracts from NDC and AD subjects

		%APP unbound to the lectin
		sAPPα		sAPPβ
Sample	APP specie	Con A	PHA	Con A	PHA
NDC	APP695	12.2 ± 1.7 [7.3–20.6]	6.6 ± 0.8 [4.3–9.4]	2.9 ± 0.8 [0.3–7.1]	2.6 ± 0.8 [0.2–6.8]
	APP-KPI	13.7 ± 2.1 [9.2–24.6]	5.7 ± 0.8 [2.8–8.1]	40.4 ± 4.6 [20.2–58.3]	37.0 ± 3.2 [22.6–51.0]
AD	APP695	7.0 ± 1.5 [2.4–12.9]	4.0 ± 0.6 [1.8–6.8]	1.2 ± 0.5 [0.1–3.7]	1.9 ± 0.3 [1.0–3.1]
	APP-KPI	7.7 ± 1.3 [4.0–12.4]	3.8 ± 0.6 [2.3–5.4]	57.1 ± 8.5 [37.6–89.0]	56.7 ± 9.7 [27.4–95.3]

The brain extracts from 7 non-demented controls (NDC) and 7 AD patients were incubated with immobilized Con A and PHA lectins. The supernatant recovered that contained the unbound protein was assayed in western blots probed with pan-specific antibodies for sAPPα and sAPPβ (see Fig. 3). The data represent the percentages (mean ± SEM) and the intervals of the unbound immunoreactivity for sAPPα and sAPPβ. These values were used to compare the differences in lectin binding between the species and groups (see Figs. 5, 6, and 7)