TABLE 1.
Bufferb | Binding condition |
125I-Vip3Aa binding (% of input) |
Ratio of specific to total binding | ||||
---|---|---|---|---|---|---|---|
pH | NaCl concn (mM) | Divalent cation | EDTA concn (mM) | Specific | Total | ||
A | 9 | 150 | 0 | 6.3 | 0 | ||
8.2 | 2.5 | 7.1 | 0.35 | ||||
B | 7.4 | 150 | 4.1 | 8.5 | 0.48 | ||
0 | 1.9 | 5.8 | 0.33 | ||||
50 | 3.5 | 7.5 | 0.47 | ||||
100 | 3.8 | 8.5 | 0.45 | ||||
300 | 2.7 | 8.1 | 0.33 | ||||
500 | 1.8 | 7.5 | 0.24 | ||||
150 | 5 | 2.8 | 7.2 | 0.39 | |||
A | 7.4 | 150 | MnCl2 (10 mM) | 0 | 21.8 | 0 | |
MnCl2 (1 mM) | 5.5 | 13.1 | 0.42 | ||||
CuSO4 (1 mM) | 0 | 8.2 | 0 | ||||
CuSO4 (0.1 mM) | 2.5 | 8.2 | 0.30 | ||||
ZnCl2 (1 mM) | 4.2 | 10.8 | 0.39 | ||||
MgCl2 (10 mM) | 1.2 | 6.9 | 0.17 | ||||
CaCl2 (1 mM) | 2.4 | 7.0 | 0.34 |
Values are the means of at least two replicates.
Buffer A is 20 mM Tris–0.1% BSA, and buffer B is 10 mM Na2HPO4/NaH2PO4-0.1% BSA.