Table I.

Comparison of the Kinetics of Trypsin Cleavage of 10 μM hDAAO in the Presence of Various Ligands

	holo-hDAAO				apo-hDAAO		hDAAO-pLG72 complex
	A1 (%)	k1 (min−1)	A2 (%)	k2 (min−1)	A1 (%)	k1 (min−1)	A1 (%)	k1 (min−1)	A2 (%)	k2 (min−1)
No ligands	68 ± 3	0.30 ± 0.04	32 ± 3	0.7 ± 0.2 ×10−2	100	0.27 ± 0.04	58 ± 8	0.55 ± 0.18	42 ± 8	6.0 ± 1.1 × 10−2
+ 0.1 mM FAD	26 ± 4	0.32 ± 0.12	74 ± 4	(≈ stable)	66 ± 5	0.34 ± 0.08	23 ± 3	0.55 ± 0.10	77 ± 3	3.3 ± 0.4 × 10−2
+ 1 mM benzoate	56 ± 3	0.48 ± 0.12	44 ± 3	(≈ stable)	100	0.27 ± 0.04	56 ± 5	0.60 ± 0.09	44 ± 6	(≈ stable)
+ 30 mM CF3-d-Ala	56 ± 4	0.32 ± 0.09	44 ± 1	(≈ stable)	100	0.27 ± 0.04	49 ± 6	0.7 ± 0.23	51 ± 4	(≈ stable)
+ 0.1 mM CPZ	68 ± 2	0.30 ± 0.02	32 ± 2	6.0 ± 1.8 ×10−2	100	0.27 ± 0.04	100	0.14 ± 0.01	—	—
+ 10 μM pLG72	42 ± 9	0.55 ± 0.18	58 ± 8	6.8 ± 1.1 ×10−2	100	0.30 ± 0.04
+ 20 μM pLG72	58 ± 6	3.6 ± 0.7	42 ± 5	0.16 ± 0.03	100	0.27 ± 0.02

Values determined by densitometric analyses of the 40-kDa band (corresponding to intact hDAAO) from SDS-PAGE analysis of the reaction mixture (see Figs. 2 and 5 for details). A₁ and A₂ represent the amplitude (percentage of proteolyzed protein) of each single phase.