ArticleJournal of biomolecular techniques : JBT2010
Comparative analysis of techniques to purify plasma membrane proteins.
Article in Journal of biomolecular techniques : JBT, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 75 citations in OpenAlex.
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- A Computational Strategy for the Rapid Identification and Ranking of Patient-Specific T Cell Receptors Bound to Neoantigens.Macromolecular rapid communications · 2024Article
- Charting the Dynamic Trophoblast Plasma Membrane Identifies LYN As a Functional Regulator of Syncytialization.ACS chemical biology · 2024Article
- Mapping the cancer surface proteome in search of target antigens for immunotherapy.Molecular therapy : the journal of the American Society of Gene Therapy · 2024Review
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- Defining the Cell Surface Cysteinome using Two-step Enrichment Proteomics.bioRxiv : the preprint server for biology · 2023Article
- Cell Surface Engineering Enables Surfaceome Profiling.ACS chemical biology · 2023Article
- Unraveling protein dynamics to understand the brain - the next molecular frontier.Molecular neurodegeneration · 2022Review
- Selective modulation of cell surface proteins during vaccinia infection: A resource for identifying viral immune evasion strategies.PLoS pathogens · 2022Article
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- A computational algorithm to assess the physiochemical determinants of T cell receptor dissociation kinetics.Computational and structural biotechnology journal · 2022Article
- A Novel Peptide-MHC Targeted Chimeric Antigen Receptor T Cell Forms a T Cell-like Immune Synapse.Biomedicines · 2021Article
- Molecular cargo in myeloid-derived suppressor cells and their exosomes.Cellular immunology · 2021Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The aim of this project was to identify the best method for the enrichment of plasma membrane (PM) proteins for proteomics experiments. Following tryptic digestion and extended liquid chromatography-tandem mass spectrometry acquisitions, data were processed using MaxQuant and Gene Ontology (GO) terms used to determine protein subcellular localization. The following techniques were examined for the total number and percentage purity of PM proteins identified: (a) whole cell lysate (total number, 84-112; percentage purity, 9-13%); (b) crude membrane preparation (104-111; 17-20%); (c) biotinylation of surface proteins with N-hydroxysulfosuccinimydyl-S,S-biotin and streptavidin pulldown (78-115; 27-31%); (d) biotinylation of surface glycoproteins with biocytin hydrazide and streptavidin pulldown (41-54; 59-85%); or (e) biotinylation of surface glycoproteins with amino-oxy-biotin (which labels the sialylated fraction of PM glycoproteins) and streptavidin pulldown (120; 65%). A two- to threefold increase in the overall number of proteins identified was achieved by using stop and go extraction tip (StageTip)-based anion exchange (SAX) fractionation. Combining technique (e) with SAX fractionation increased the number of proteins identified to 281 (54%). Analysis of GO terms describing these proteins identified a large subset of proteins integral to the membrane with no subcellular assignment. These are likely to be of PM location and bring the total PM protein identifications to 364 (68%). This study suggests that selective biotinylation of the cell surface using amino-oxy-biotin in combination with SAX fractionation is a useful method for identification of sialylated PM proteins.
Indexed as
Identifiers
20808639PMC2922835W85804856What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.