English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/12922
Compartir / Impacto:
Add this article to your Mendeley library MendeleyBASE
Citado 33 veces en Web of Knowledge®  |  Pub MebCentral Ver citas en PubMed Central  |  Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL

capillary electrophoresis-mass spectrometry of zein proteins from conventional and transgenic maize

AutorErny, Guillaume L.; Marina, María Luisa ; Cifuentes, Alejandro
Palabras claveprotein separation
Bt corn
capillary coating
food analysis
Fecha de publicaciónnov-2007
CitaciónElectrophoresis 28 (2007) 4192-4201
ResumenIn this work, an original capillary electrophoresis-mass spectrometry (CE-MS) method has been developed to analyze the complex zein proteins fraction from maize. A thorough optimization of i) zein proteins extraction, ii) CE separation and iii) electrospray-mass spectrometry (ESI-MS) detection is carried out in order to obtain highly informative CE-MS profiles of this fraction. The developed CE-MS method provides good separation of multiple zein proteins based on their electrophoretic mobilities as well as adequate characterization of these proteins based on their relative molecular mass (Mr). Zein proteins with small Mr differences (below 100 Da) were easily separated and successfully analyzed by CE-MS. Thus, apart of the so-called 15-kDa--zein and 16-kDa--zein, which are demonstrated to be formed by a heterogeneous group of proteins, numerous -zeins belonging to the 19 and 22-kDa fraction were also identified for the first time in this work. The usefulness of this CE-MS method was corroborated by comparing the zein-proteins fingerprint of various maize lines including transgenic and their corresponding non-transgenic isogenic lines cultivated under the same conditions.
Versión del editor10.1002/elps.200700323
Aparece en las colecciones: (IFI) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
Electrophoresis-2007-4192.doc497,5 kBMicrosoft WordVisualizar/Abrir
Mostrar el registro completo

NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.