biostudies-literatureRuan SHangzhou Agricultural and Social Development Scientific ResearchHangzhou Academy of Agricultural SciencesNational Key Research and Development Program of ChinaHangzhou Great Science and Technology Innovation100002https://www.ebi.ac.uk/biostudies/studies/S-EPMC8991595biostudies-literatureUnknown1Ethanol-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 Food chemistry. Molecular sciencesProteomic analysis of 2-chloroethanol extracts of rice (<i>Oryza sativa</i> L.) seeds.PMC89915952017YFD020090020172015A022019HNCT-2820131812A02Qiu JHu WRuan STong JMa HXiao WYing WChen HfalseProteomic analysis of 2-chloroethanol extracts of rice (<i>Oryza sativa</i> L.) seeds.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 2020-01-01T00:00:00Z2020 Oct2026-04-08T10:36:02.366Z2025-02-19T01:11:02.206ZS-EPMC89915953541561910.1016/j.fochms.2020.100002