Cell Surface Protein Biotinylation and Analysis
نویسندگان
چکیده
منابع مشابه
Cell-surface biotinylation of GLUT4 using bis-mannose photolabels.
New cell-impermeant bis-mannose photolabels have been developed with biotinyl groups attached to 4-(1-azi-2,2,2-trifluoroethyl)-benzoyl-1, 3-bis(d-mannos-4-yloxy)-2-propylamine (ATB-BMPA) by either a polyethoxy spacer (Bio-ATB-BMPA) or an additional hexanoic acid spacer (Bio-LC-ATB-BMPA). The half-maximal inhibition constants, Ki values, for inhibition of glucose transport activity in insulin-s...
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The biotinylating reagent succinimidyl 6-(biotinamido)hexanoate was used to label the cell surfaces of the cosmopolitan, marine, eukaryotic microorganism Emiliania huxleyi under different growth conditions. Proteins characteristic of different nutrient conditions could be identified. In particular, a nitrogen-regulated protein, nrp1, has an 82-kDa subunit that is present under nitrogen limitati...
متن کاملBiotinylation and Purification of Surface-exposed Helicobacter pylori Proteins.
Interactions between pathogenic bacteria and host cells are often mediated by proteins found on the surfaces of the bacteria. The Gram-negative bacterium Helicobacter pylori is predicted to produce at least 50 surface-exposed outer membrane proteins, but there has been relatively little progress in experimentally analyzing the cell-surface proteome of this organism. Herein, we describe in detai...
متن کاملIn vivo intravascular biotinylation of Schistosoma bovis adult worms and proteomic analysis of tegumental surface proteins.
UNLABELLED Schistosoma bovis is a blood-dwelling fluke of ruminants that lives for years inside the vasculature of their hosts. The parasite tegument covers the surface of the worms and plays a key role in the host-parasite relationship. The parasite molecules expressed at the tegument surface are potential targets for immune or drug intervention. The purpose of this work was the identification...
متن کاملA surface-focused biotinylation procedure identifies the Yersinia pestis catalase KatY as a membrane-associated but non-surface-located protein.
This study identified major surface proteins of the plague bacterium Yersinia pestis. We applied a novel surface biotinylation method, followed by NeutrAvidin (NA) bead capture, on-bead digestion, and identification by liquid chromatography-tandem mass spectrometry (LC-MS-MS). The use of stachyose during biotinylation focused the reaction to the surface. Coupled with NA pulldown and immunoblot ...
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ژورنال
عنوان ژورنال: BIO-PROTOCOL
سال: 2013
ISSN: 2331-8325
DOI: 10.21769/bioprotoc.857