Publikation: Hydrophobic and hydrophilic radio-iodination, crosslinking, and differential extraction of cell surface proteins in Paramecium tetraurelia cells
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We combined widely different biochemical methods to analyze proteins of the cell surface of P. tetraurelia since so far one can isolate only a subfraction of cell membrane vesicles enriched in the GPI-anchored surface antigens ( immoblization or i-AGs ). We also found that i-AGs may undergo partial degradation by endogenous proteases. Genuine intrinsic membrane proteins were recognized particularly with lipophilic 5-[125I]-iodonaphthalene-1-azide (INA) labeling which reportedly sees integral proteins and cytoplasmic cell membrane-associated proteins. With INA (+DTT), bands of ≤ 55 kDa were similar as with hydrophilic iodogen (+DTT), but instead of large size bands including i-AGs, a group of 122, 104 and 94 kDa appeared. Several bands of the non i-AG type are compatible with integral (possibly oligomeric) or associated proteins of the cell membrane of established molecular identity, as we discuss. In summary, we can discriminate between i-AGs and some functionally important minor cell membrane components. Our methodical approach might be relevant also for an analysis of some related protozoan parasites.
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FLÖTENMEYER, Matthias, Massoud MOMAYEZI, Helmut PLATTNER, 1999. Hydrophobic and hydrophilic radio-iodination, crosslinking, and differential extraction of cell surface proteins in Paramecium tetraurelia cells. In: Journal of Membrane Biology. 1999, 172(1), pp. 77-88. ISSN 0022-2631. eISSN 1432-1424. Available under: doi: 10.1007/s002329900585BibTex
@article{Flotenmeyer1999Hydro-7487, year={1999}, doi={10.1007/s002329900585}, title={Hydrophobic and hydrophilic radio-iodination, crosslinking, and differential extraction of cell surface proteins in Paramecium tetraurelia cells}, number={1}, volume={172}, issn={0022-2631}, journal={Journal of Membrane Biology}, pages={77--88}, author={Flötenmeyer, Matthias and Momayezi, Massoud and Plattner, Helmut} }
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