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. 2018 Jun 22;293(33):12663–12680. doi: 10.1074/jbc.RA117.000871

Table 1.

Inhibition, binding, and hydrolysis constants of APPIWT and APPI-4M

APPI variant Ki a KDb konb koffb Turnover timec
nm nm m1 s1 s1 h
APPIWT 2.24 ± 0.11d 5.29 (1.96 ± 0.01) × 105 (10.40 ± 0.02) × 10−4 16.62 ± 0.05
APPI-4M 0.16 ± 0.06 0.04 (3.17 ± 0.01) × 105 (1.15 ± 0.06) × 10−5 230.07 ± 40.90

a Data were determined by slow tight binding inhibition assays.

b Data were determined by SPR.

c Data were determined by HPLC.

d Data were previously reported in Ref. 50.