{"doi":"10.1155/s1110724303209244","title":"Selective Enrichment of Membrane Proteins by Partition Phase Separation for Proteomic Studies","abstract":"<jats:p>The human proteome project will demand faster, easier, and more\nreliable methods to isolate and purify protein targets. Membrane\nproteins are the most valuable group of proteins since they are\nthe target for 70–80% of all drugs. Perbio Science has\ndeveloped a protocol for the quick, easy, and reproducible\nisolation of integral membrane proteins from eukaryotic cells.\nThis procedure utilizes a proprietary formulation to facilitate\ncell membrane disruption in a mild, nondenaturing environment and\nefficiently solubilizes membrane proteins. The technique utilizes\na two‐phase partitioning system that enables the class separation\nof hydrophobic and hydrophilic proteins. A variety of protein\nmarkers were used to investigate the partitioning efficiency of\nthe membrane protein extraction reagents (Mem‐PER) (Mem‐PER is a\nregistered trademark of Pierce Biotechnology, Inc) system. These\nincluded membrane proteins with one or more transmembrane\nspanning domains as well as peripheral and cytosolic proteins.\nBased on densitometry analyses of our Western blots, we obtained\nexcellent solubilization of membrane proteins with less than\n10% contamination of the hydrophobic fraction with hydrophilic\nproteins. Compared to other methodologies for membrane protein\nsolubilization that use time‐consuming protocols or expensive and\ncumbersome instrumentation, the Mem‐PER reagents system for\neukaryotic membrane protein extraction offers an easy, efficient,\nand reproducible method to isolate membrane proteins from\nmammalian and yeast cells.</jats:p>","journal":"BioMed Research International","year":2003,"id":651593,"datarank":0.611630616585858,"base_score":4.07753744390572,"endowment":4.07753744390572,"self_citation_contribution":0.611630616585858,"citation_network_contribution":0.0,"self_endowment_contribution":0.611630616585858,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":58,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1699431,"name":"Betsy Benton","orcid":null,"position":1,"is_corresponding":false},{"id":1699433,"name":"Ray Ignacio","orcid":null,"position":2,"is_corresponding":false},{"id":1699435,"name":"Barbara Kaboord","orcid":null,"position":3,"is_corresponding":false},{"id":845596,"name":"M. Walid Qoronfleh","orcid":"0000-0001-6757-1922","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Selective Enrichment of Membrane Proteins by Partition Phase Separation for Proteomic Studies","abstract":"<jats:p>The human proteome project will demand faster, easier, and more\nreliable methods to isolate and purify protein targets. Membrane\nproteins are the most valuable group of proteins since they are\nthe target for 70–80% of all drugs. Perbio Science has\ndeveloped a protocol for the quick, easy, and reproducible\nisolation of integral membrane proteins from eukaryotic cells.\nThis procedure utilizes a proprietary formulation to facilitate\ncell membrane disruption in a mild, nondenaturing environment and\nefficiently solubilizes membrane proteins. The technique utilizes\na two‐phase partitioning system that enables the class separation\nof hydrophobic and hydrophilic proteins. A variety of protein\nmarkers were used to investigate the partitioning efficiency of\nthe membrane protein extraction reagents (Mem‐PER) (Mem‐PER is a\nregistered trademark of Pierce Biotechnology, Inc) system. These\nincluded membrane proteins with one or more transmembrane\nspanning domains as well as peripheral and cytosolic proteins.\nBased on densitometry analyses of our Western blots, we obtained\nexcellent solubilization of membrane proteins with less than\n10% contamination of the hydrophobic fraction with hydrophilic\nproteins. Compared to other methodologies for membrane protein\nsolubilization that use time‐consuming protocols or expensive and\ncumbersome instrumentation, the Mem‐PER reagents system for\neukaryotic membrane protein extraction offers an easy, efficient,\nand reproducible method to isolate membrane proteins from\nmammalian and yeast cells.</jats:p>","is_dataset_classified":null,"base_score":4.07753744390572,"endowment":4.07753744390572,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"14615633","pmcid":"PMC514269","openalex_id":"https://openalex.org/W2015829278","authors":[],"funders":[],"total_grants":0,"fwci":0.9954,"citation_percentile":0.72747857,"influential_citations":0,"citation_trend":[{"year":2012,"count":1},{"year":2013,"count":3},{"year":2014,"count":4},{"year":2015,"count":1},{"year":2016,"count":2},{"year":2017,"count":2},{"year":2018,"count":2},{"year":2019,"count":2},{"year":2020,"count":1},{"year":2021,"count":1},{"year":2022,"count":4},{"year":2023,"count":6},{"year":2024,"count":4},{"year":2025,"count":3}],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"https://downloads.hindawi.com/journals/bmri/2003/505318.pdf","host_type":"journal"},{"url":"https://downloads.hindawi.com/journals/bmri/2003/505318.pdf","host_type":"publisher"},{"url":"http://downloads.hindawi.com/journals/bmri/2003/505318.pdf","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/pdf/10.1155/S1110724303209244","host_type":"publisher"},{"url":"https://doi.org/10.1155/s1110724303209244","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/14615633","host_type":"repository"},{"url":"https://doaj.org/article/10ca6069bbca422389164d40f9ec5a17","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/514269","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC514269","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC514269?pdf=render","host_type":"Europe_PMC"}],"fields_of_study":["Mass Spectrometry Techniques and Applications","Lipid Membrane Structure and Behavior","Advanced Proteomics Techniques and Applications"],"mesh_terms":[],"keywords":["Partition (number theory)","Separation (statistics)","Chemistry","Membrane protein","Chromatography","Membrane","Biochemistry","Computer science","Mathematics"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-10T10:05:34.558524Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}