{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ruan S"],"funding":["Hangzhou Agricultural and Social Development Scientific Research","Hangzhou Academy of Agricultural Sciences","National Key Research and Development Program of China","Hangzhou Great Science and Technology Innovation"],"pagination":["100002"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8991595"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["1"],"pubmed_abstract":["Ethanol-soluble proteins, including prolamins, are one of the most important seed proteins in rice (<i>Oryza sativa</i> L.). However, little is known about the proteomic profile of ethanol-soluble protein fraction extracted from rice grain. In this work, the differential profile of ethanol-soluble proteins extracted by 2-chloroethanol and ethanol has been documented. Proteome analysis utilizing LC-MS/MS identified a total of 64 unique proteins in the 2-chloroethanol extract of rice seeds. The majority of these proteins had low molecular weight ranging from 10 to 25 kD and isoelectric point (pI) in mid-acidic (pH 5-pH 7) and mid-basic (pH 7-pH 9) ranges. Database searches combined with transmembrane domain (TMD) analysis revealed that >70% of identified proteins were hydrophobic, i.e., had "],"journal":["Food chemistry. Molecular sciences"],"pubmed_title":["Proteomic analysis of 2-chloroethanol extracts of rice (<i>Oryza sativa</i> L.) seeds."],"pmcid":["PMC8991595"],"funding_grant_id":["2017YFD0200900","20172015A02","2019HNCT-28","20131812A02"],"pubmed_authors":["Qiu J","Hu W","Ruan S","Tong J","Ma H","Xiao W","Ying W","Chen H"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic analysis of 2-chloroethanol extracts of rice (<i>Oryza sativa</i> L.) seeds.","description":"Ethanol-soluble proteins, including prolamins, are one of the most important seed proteins in rice (<i>Oryza sativa</i> L.). However, little is known about the proteomic profile of ethanol-soluble protein fraction extracted from rice grain. In this work, the differential profile of ethanol-soluble proteins extracted by 2-chloroethanol and ethanol has been documented. Proteome analysis utilizing LC-MS/MS identified a total of 64 unique proteins in the 2-chloroethanol extract of rice seeds. The majority of these proteins had low molecular weight ranging from 10 to 25 kD and isoelectric point (pI) in mid-acidic (pH 5-pH 7) and mid-basic (pH 7-pH 9) ranges. Database searches combined with transmembrane domain (TMD) analysis revealed that >70% of identified proteins were hydrophobic, i.e., had ","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Oct","modification":"2026-04-08T10:36:02.366Z","creation":"2025-02-19T01:11:02.206Z"},"accession":"S-EPMC8991595","cross_references":{"pubmed":["35415619"],"doi":["10.1016/j.fochms.2020.100002"]}}