English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/32751
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

Biochemical Characterization and Cellular Localization of 11S Type Storage Proteins in Olive (Olea europaea L.) Seeds

AuthorsAlché Ramírez, Juan de Dios; Jiménez-López, José Carlos; Wang, Wei; Castro López, Antonio Jesús; Rodríguez García, María I.
KeywordsCotyledon
Endosperm
Olea europaea L.
Olive tree
protein bodies
11S storage protein
Issue Date2006
PublisherAmerican Chemical Society
CitationJournal of Agricultural and Food Chemistry 54(15): 5562-5570 (2006)
AbstractThe composition of seed storage proteins (SSPs) in olive endosperm and cotyledon has been analyzed. Precursor forms of these proteins are made up of individual proteins, which have been purified to homogeneity and further named p1−p5 (20.5, 21.5, 25.5, 27.5, and 30 kDa, respectively). N-terminal sequences of p1 and p2 proteins displayed relevant homology to the basic subunit of the 11S family of plant SSPs (legumins). Two-dimensional polyacrylamide gel electrophoresis experiments allowed us to verify the basic character of p1 and p2 and the acidic character of p3, p4, and p5 proteins. In addition, the putative presence of highly similar isoforms or posttranslational modifications of these polypeptides was detected. As a result, a model describing the putative association of p1−p5 proteins into subunits of α(acidic)/β(basic) type has been proposed. Solubility experiments have shown that the majority of these olive seed proteins from the 11S storage protein family are extracted with aqueous alcohol and only partially with water and diluted saline solutions, therefore suggesting their similarity to prolamines. Moreover, no visible differences were found in either subunit composition or 11S proteins mass among six olive cultivars examined. This result suggests that the synthesis of storage proteins is highly conserved in this plant species. By using a rabbit antiserum raised to p1 protein, the proteins have also been immunolocalized in olive seed tissues, showing that they accumulate in conspicuous protein bodies present in both the endosperm and the cotyledon.
Description9 páginas, 10 figuras, 2 tablas.
Publisher version (URL)http://dx.doi.org/10.1021/jf060203s
URIhttp://hdl.handle.net/10261/32751
DOI10.1021/jf060203s
ISSN0021-8561
Appears in Collections:(EEZ) Artículos
Files in This Item:
File Description SizeFormat 
jf060203s.pdf483,16 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.