Kinetic parameters for the acid-resistant binding of 125I-ADAB and 125I-ADAMB to TM-BBB4 cells The maximal binding capacity (Bmax), the half-saturation constant (Kd), and the nonspecific binding (α) were estimated by nonlinear least-squares analysis using Prism 3 software from the data in Fig. 2. Each value represents the mean ± calculated S.D.
Peptides | Bmax | Kd | α | Bmax/Kd |
|---|---|---|---|---|
| pmol/mg protein | μM | μ1/mg protein | μ1/mg protein | |
| 125I-ADAB | 12.8 ± 2.6 | 3.76 ± 0.83 | 1.43 ± 0.09 | 3.4 |
| 125I-ADAMB | 22.5 ± 11.9 | 5.68 ± 1.75 | 1.98 ± 0.29 | 4.0 |