Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/197324
Type: Artigo de periódico
Title: The Use Of Asb-14 In Combination With Chaps Is The Best For Solubilization Of Human Brain Proteins For Two-dimensional Gel Electrophoresis.
Author: Martins-de-Souza, Daniel
Martins, Daniel
Menezes de Oliveira, Bruno
dos Santos Farias, Alessandro
Horiuchi, Ricardo Shiniti Oka
Crepaldi Domingues, Cleyton
de Paula, Eneida
Marangoni, Sérgio
Gattaz, Wagner Farid
Dias-Neto, Emmanuel
Camillo Novello, José
Abstract: Protein extraction is the most important step to reveal a proteome by Two-Dimensional Gel Electrophoresis. Usually, the urea/thiourea based standard protein extraction buffer (SB) is combined with detergents with the aim of achieving better resolution and solubilization of different classes of proteins. In order to produce better gels and achieve the greatest spot resolution of Human Brain Proteins, comparisons using 2-DE of extracted proteins from Human Brain Frontal Cortex with SB constituents (7M Urea, 2M Thiourea and 100mM DTT) were made, using different detergent compositions in the buffer. SB preparations in combination with CHAPS and ASB-14 as well as with ASB-16 (reported for the first time in 2-DE experiments) have been tested. Our results confirm that the most efficient solubilizing solution for 2-DE analysis of cytosolic and membrane Human Brain Proteins is SB combined with 4% CHAPS and 2% ASB-14.
Subject: Betaine
Brain Chemistry
Cholic Acids
Detergents
Electrophoresis, Gel, Two-dimensional
Humans
Proteins
Solubility
Citation: Briefings In Functional Genomics & Proteomics. v. 6, n. 1, p. 70-5, 2007-Mar.
Rights: fechado
Identifier DOI: 10.1093/bfgp/elm009
Address: http://www.ncbi.nlm.nih.gov/pubmed/17556486
Date Issue: 2007
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File SizeFormat 
pmed_17556486.pdf279.31 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.