Table 1.
Values of Kd from previous studies
| Reference | Protease | pH | Kd | τ1/2 (sec) | Remark |
| Holzman et al. 1991 | HIV-2 | 4.5 | 87 μM | ||
| 7.5 | 28 μM | ||||
| Grant et al. 1992 | HIV-1 | 5.0 | <10 nM | ||
| Towler et al. 1998 | HIV-1 | 7.0 | 9 μM | ||
| HERV-K10 | 7.0 | 52.5 μM | |||
| Xie et al. 1999 | HIV-1 | 7.0 | 52.7 μM | Autolysis products interferred, Kd taken as upper limit | |
| Stříšovský et al. 2000 | HIV-1 | 6.0 | 77 μM | ||
| Cheng et al. 1990 | HIV-1 | 7.0 | 50 nM | 198 | |
| Zhang et al. 1991 | HIV-1 | 3.6 nM | Very fast processes assumed | ||
| Jordan et al. 1992 | HIV-1 | <1 nM | |||
| HIV-2 | <1 nM | ||||
| Darke et al. 1994 | HIV-1 | 6.5 | 16 nM | Fluorogenic inhibitor used | |
| 7.0 | 39 nM | ||||
| Pargellis et al. 1994 | HIV-1 | 5.5 | 5.2 nM | 533 | 0 M NaCl |
| 4.0 nM | 745 | 1.5 M NaCl | |||
| Kuzmič et al. 1993 | HIV-1 | 6.4 | 440 nM | 23.9 | |
| Uhlíková et al. 1996 | HIV-1 | 6.4 | 112 nM | Integral kinetics | |
| 4.5 | 19 nM |
The top part of the table shows the results of sedimentation studies; the bottom part the results of kinetic assays. τ1/2 is the halftime of dimer dissociation.