Abstract
Acylated pardaxin is translocated through the cytoplasmic membrane and is accumulated in the nucleoli of NG108-15 and chromaffin cells. The uptake is time- and dose-dependent and temperature-sensitive. However, the binding of acylated 125I-pardaxin cannot be reduced by competition with pardaxin acylated with Rudinger's reagent. In this respect, acylated pardaxin resembles the Tat protein 37-71 fragment. Metabolic inhibitors do not significantly reduce the uptake of acylated 125I-pardaxin. Acylated pardaxin might be useful as a vector to translocate other molecules. Copyright (C) 1998 Federation of European Biochemical Societies.
| Original language | English |
|---|---|
| Pages (from-to) | 131-134 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 440 |
| Issue number | 1-2 |
| DOIs | |
| State | Published - 27 Nov 1998 |
Keywords
- Pardaxin uptake
- Peptide uptake