Hydrophobic and Hydrophilic Radio-Iodination, Crosslinking, and Differential Extraction of Cell Surface Proteins in Paramecium tetraurelia Cells

Hydrophobic and Hydrophilic Radio-Iodination, Crosslinking, and Differential Extraction of Cell... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Hydrophobic and Hydrophilic Radio-Iodination, Crosslinking, and Differential Extraction of Cell Surface Proteins in Paramecium tetraurelia Cells

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Publisher
Springer-Verlag
Copyright
Copyright © Inc. by 1999 Springer-Verlag New York
Subject
Life Sciences; Biochemistry, general; Human Physiology
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s002329900585
Publisher site
See Article on Publisher Site

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