Table 2.
ANS Fluorescence in the Presence of WT and Mutant Forms of Lipid-Free apoA-I and “Reference Proteins”. Trp Fluorescence of WT and Mutant Forms of Lipid-free apoA-I.
| Protein | WMF c (nm) | I c (relative units d) | I c (relative units e) | WMF f (nm) |
|---|---|---|---|---|
| WT b | 479 (-37)c | 4.5 | 1.0 | 335 |
| apoA-I[D102A/D103A]b | 475 (-41) | 6.3 | 1.3 | 338 |
| apoA-I[R116V/ K118A]b | 479 (-37) | 4.0 | 0.9 | 336 |
| apoA-I[R160V/H162A]b | 475 (-41) | 6.5 | 1.4 | 337 |
| apoA-I[Δ(61-78)]b | 476 (-40) | 7.0 | 1.6 | * |
|
|
|
|
|
|
| WT a | 480 (-36) | 4.3 | 1.0 | 335 |
| apoA-I[E110A/E111A] a | 477 (-39) | 6.8 | 1.5 | 337 |
| apoA-I[Δ(121-142)] a | 492 (-24) | 3.3 | 0.7 | 335 |
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|
|
|
|
| Bovine Serum Albumin | 475 (-41) | 9.5 | 2.1 | N/A |
| Carbonic Anhydrase | 516 | 1.0 | 0.2 | N/A |
| ANS in buffer alone | 516 | 1.0 | 0.2 | N/A |
Proteins were expressed in the adenovirus
Proteins were expressed in the baculovirus expression system.
ANS fluorescence in the presence of 0.05 mg/ml of WT or the mutant forms of apoA-I, carbonic anhydrase or bovine serum albumin, or in PBS buffer alone. Values in parentheses show changes in WMF compared to that for ANS in PBS buffer.
ANS fluorescence intensity in relative units compared to the fluorescence in the buffer alone.
ANS fluorescence intensity in relative units compared to the fluorescence in the presence of WT expressed in the baculovirus expression system.
Intrinsic Trp fluorescence of WT and mutant apoA-I in PBS.
WMF for the apoA-I[Δ(61-78)] was not determined because of the lack of Trp72 in this mutant.