alexa Gel-based Proteomic Characterization of Soluble and Ins
ISSN: 0974-276X

Journal of Proteomics & Bioinformatics
Open Access

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Research Article

Gel-based Proteomic Characterization of Soluble and Insoluble Fraction Proteins in Rat Spinal Cord

Shuguang Yang1#, Qinxue Ding1, 2#, Yaojun Guo3, Congjian Zhao1, Yufeng Jia1, Haiping Que1, Hongxia Wang4, Kaihua Wei4, Dacheng He2, Shuqian Jing1, 5, Shaojun Liu1*

1State Key Laboratory of Proteomics and Department of Neurobiology, Department of Neurobiology, Institute of Basic Medical Sciences, Beijing 100850, P.R. China

2Institute of Cell Biology, Beijing Normal University, Beijing 100875, P.R. China

3Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China

4China National Center of Biomedical Analysis, Beijing 100850, P.R. China

5Department of Clinical Immunology, Amgen Inc., One Amgen Center Drive, Thousand Oaks, CA, USA

#These authors contributed equally to this work

*Corresponding Author:
Professor Shaojun Liu
State Key Laboratory of Proteomics and Department of Neurobiology
Neurobiology Department
Institute of Basic Medical Sciences
Beijing, 100850, P.R.China
Tel: +86-10-66931304
Fax: 86-10-68213039
E-mail: [email protected]

Received Date: January 22, 2010; Accepted Date: February 23, 2010; Published Date: February 23, 2010

Citation: Yang S, Ding Q, Guo Y, Zhao C, Jia Y, et al. (2010) Gel-based Proteomic Characterization of Soluble and Insoluble Fraction Proteins in Rat Spinal Cord. J Proteomics Bioinform 3: 074-081. doi: 10.4172/jpb.1000124

Copyright: © 2010 Yang S, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permitsunrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 

Abstract

Fractionation efficiency and protein characterization of neural soluble and insoluble proteins by sequential extraction was scrutinized by gel-based proteomic analysis. Spinal cord proteins of adult rats were first extracted with aqueous buffer (fraction A), followed by standard (fraction B) or modified (fraction C) enhanced solutions. Of the top 30 most abundant proteins in fractions A, B and C, the percentage of cytoplasmic proteins was 74% (28/38) , 37% (14/38) and 42% (15/36), respectively; membrane organellar proteins accounted for 8% (3/38), 45% (17/38), and 44% (16/36); membrane proteins accounted for 13% (5/38), 18% (7/38) and 14% (5/36). The number of hydrophobic domains was 5, 15 and 9. Shared proteins in three fractions were only 13%. When additional less abundant 30 spots enriched the insoluble fraction C were characterized, membrane proteins accounted for 31%, among which 83% were peripheral membrane proteins and 17% were integral membrane proteins. Functional analysis also revealed some difference between different fractions although all fractionated proteins are involved in energy metabolism, redox regulation, signal transduction and cellular architecture.

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