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 |
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Pages (from-to) | 131-134 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 440 |
Issue number | 1-2 |
DOIs | |
State | Published - 27 Nov 1998 |
Externally published | Yes |
Bibliographical note
Funding Information:This work was supported in part by a grant from the Lower Saxony-Israel Research Fund to J.H., P.L., and H.W.
Funding
This work was supported in part by a grant from the Lower Saxony-Israel Research Fund to J.H., P.L., and H.W.
Funders | Funder number |
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Lower Saxony-Israel Research Fund |
Keywords
- Pardaxin uptake
- Peptide uptake