Literature DB >> 16674118

Use of solution-IEF-fractionation leads to separation of 2673 mouse brain proteins including 255 hydrophobic structures.

Jae-Kyung Myung1, Gert Lubec.   

Abstract

Analyzing complex protein mixtures on a single gel does not allow separation of many extracted proteins. Herein, we tried a prefractionation approach and mouse brain proteins were separated on a narrow pH range ZOOM-IEF Fractionator (MicroSol-IEF device) and run on two-dimensional gel electrophoresis. A total number of 2673 protein spots including 255 hydrophobic structures were successfully analyzed by mass spectrometry. This nonsophisticated approach to increase protein identification of a brain protein extract is a step forward in neurochemistry.

Entities:  

Mesh:

Substances:

Year:  2006        PMID: 16674118     DOI: 10.1021/pr060015h

Source DB:  PubMed          Journal:  J Proteome Res        ISSN: 1535-3893            Impact factor:   4.466


  3 in total

1.  Combining isoelectric point-based fractionation, liquid chromatography and mass spectrometry to improve peptide detection and protein identification.

Authors:  Stephanie M Cologna; William K Russell; Peniel J Lim; Gyula Vigh; David H Russell
Journal:  J Am Soc Mass Spectrom       Date:  2010-04-24       Impact factor: 3.109

2.  Microscale solution isoelectric focusing as an effective strategy enabling containment of hemeoglobin-derived products for high-resolution gel-based analysis of the Plasmodium falciparum proteome.

Authors:  Niroshini Nirmalan; Fiona Flett; Tom Skinner; John E Hyde; Paul F G Sims
Journal:  J Proteome Res       Date:  2007-08-14       Impact factor: 4.466

3.  A proteomic analysis of Curcuma comosa Roxb. rhizomes.

Authors:  Apaporn Boonmee; Chantragan Srisomsap; Daranee Chokchaichamnankit; Aphichart Karnchanatat; Polkit Sangvanich
Journal:  Proteome Sci       Date:  2011-07-29       Impact factor: 2.480

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.