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Proteomic analysis of 2-chloroethanol extracts of rice (Oryza sativa L.) seeds

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Title: Proteomic analysis of 2-chloroethanol extracts of rice (Oryza sativa L.) seeds
Authors: Songlin Ruan, Wenfei Xiao, Jieren Qiu, Weimin Hu, Wu Ying, Huizhe Chen, Jianxin Tong, Huasheng Ma
Source: Food Chemistry: Molecular Sciences, Vol 1, Iss , Pp 100002- (2020)
Publisher Information: Elsevier, 2020.
Publication Year: 2020
Collection: LCC:Nutrition. Foods and food supply
Subject Terms: Rice seed, Ethanol-soluble protein, Proteomic analysis, Seed storage protein, Protease inhibitors, Nutrition. Foods and food supply, TX341-641
More Details: Ethanol-soluble proteins, including prolamins, are one of the most important seed proteins in rice (Oryza sativa 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 at least one TMD. Gene ontology classification and enrichment analysis showed that the identified proteins were involved in13 types of biological processes, 5 types of cell components, and 17 types of molecular functions. These results were significant based on the hyper p-value of
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2666-5662
Relation: http://www.sciencedirect.com/science/article/pii/S2666566220300022; https://doaj.org/toc/2666-5662
DOI: 10.1016/j.fochms.2020.100002
Access URL: https://doaj.org/article/d2a220b59c3b4ea8be1aa4b83c75586d
Accession Number: edsdoj.2a220b59c3b4ea8be1aa4b83c75586d
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  Data: Proteomic analysis of 2-chloroethanol extracts of rice (Oryza sativa L.) seeds
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  Data: <searchLink fieldCode="AR" term="%22Songlin+Ruan%22">Songlin Ruan</searchLink><br /><searchLink fieldCode="AR" term="%22Wenfei+Xiao%22">Wenfei Xiao</searchLink><br /><searchLink fieldCode="AR" term="%22Jieren+Qiu%22">Jieren Qiu</searchLink><br /><searchLink fieldCode="AR" term="%22Weimin+Hu%22">Weimin Hu</searchLink><br /><searchLink fieldCode="AR" term="%22Wu+Ying%22">Wu Ying</searchLink><br /><searchLink fieldCode="AR" term="%22Huizhe+Chen%22">Huizhe Chen</searchLink><br /><searchLink fieldCode="AR" term="%22Jianxin+Tong%22">Jianxin Tong</searchLink><br /><searchLink fieldCode="AR" term="%22Huasheng+Ma%22">Huasheng Ma</searchLink>
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  Data: Food Chemistry: Molecular Sciences, Vol 1, Iss , Pp 100002- (2020)
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  Data: <searchLink fieldCode="DE" term="%22Rice+seed%22">Rice seed</searchLink><br /><searchLink fieldCode="DE" term="%22Ethanol-soluble+protein%22">Ethanol-soluble protein</searchLink><br /><searchLink fieldCode="DE" term="%22Proteomic+analysis%22">Proteomic analysis</searchLink><br /><searchLink fieldCode="DE" term="%22Seed+storage+protein%22">Seed storage protein</searchLink><br /><searchLink fieldCode="DE" term="%22Protease+inhibitors%22">Protease inhibitors</searchLink><br /><searchLink fieldCode="DE" term="%22Nutrition%2E+Foods+and+food+supply%22">Nutrition. Foods and food supply</searchLink><br /><searchLink fieldCode="DE" term="%22TX341-641%22">TX341-641</searchLink>
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  Data: Ethanol-soluble proteins, including prolamins, are one of the most important seed proteins in rice (Oryza sativa 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 at least one TMD. Gene ontology classification and enrichment analysis showed that the identified proteins were involved in13 types of biological processes, 5 types of cell components, and 17 types of molecular functions. These results were significant based on the hyper p-value of
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