REHABER, P and SECKLER, R and JAENICKE, R (1991) INTERMOLECULAR INTERACTIONS INVOLVED IN THE ASSOCIATION OF THE VARIANT SURFACE GLYCOPROTEIN OF TRYPANOSOMA-BRUCEI. BIOLOGICAL CHEMISTRY HOPPE-SEYLER, 372 (8). pp. 593-598. ISSN 0177-3593,
Full text not available from this repository.Abstract
Trypanosomes in their mammalian host are covered by the densely packed variant surface glycoprotein (VSG). Depending on the presence or absence of a glycosyl-phosphatidyl inositol anchor, VSG is accessible as soluble globular protein (sVSG), or as insoluble membrane form (mfVSG). In order to get insight into the two-dimensional association of VSG within the surface layer, protein-protein interactions were investigated in a wide range of protein concentrations. No self-assembly of sVSG could be detected even at protein concentrations close to the local packing in the surface layer. The absence of preferential interactions with soybean phospholipid or lysolecithin monolayers (spread on a Langmuir trough) suggests that the soluble form of the protein is not integrated into a model lipid-water interface. Thus, the two-dimensional arrangement of the protein in situ seems to be determined by hydrophobic interactions of the lipid components rather than protein-lipid interactions. In contrast to sVSG, the membrane form (mfVSG) undergoes aggregation and shows a strong tendency to adsorb to surfaces and chromatographic matrices, thus interfering with standard techniques of protein purification.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PHOSPHATIDYLINOSITOL MEMBRANE ANCHOR; PURIFICATION; FORM; PROTEINS; COAT; TRYPANOSOMA-BRUCEI; VARIANT SURFACE GLYCOPROTEIN; PROTEIN-PROTEIN INTERACTIONS; CELL MEMBRANE; GLYCOSYL-PHOSPHATIDYL INOSITOL ANCHOR |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:46 |
| URI: | https://pred.uni-regensburg.de/id/eprint/54927 |
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