Biochemistry & Physiology: Open Access
Open Access

Research Article

Proteome Analysis on Proteins Sequentially Extracted from Loach (Misgurnus anguillicaudatus)

Yanlei Yu¹, Ning Zang², Fuming Zhang^3*, Robert J Linhardt³ and Hong Zhang^1*

¹School of Food Science and Biological Engineering, Zhejiang Gongshang University, China

²Medical Scientific Research Center, Guangxi Medical University, Nanning, China

³Departments of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, New York, USA

*Corresponding Author:

Hong Zhang
School of Food Science and Biological Engineering
Zhejiang Gongshang University, Hangzhou
Zhejiang, 310018, China
Tel: +86-571-2800-8966
Email: hongzh1316@mail.zjgsu.edu.cn
Fuming Zhang
Department of Chemical and Biological Engineering
Center for Biotechnology and Interdisciplinary Studies
Rensselaer Polytechnic Institute, Troy
NY12180, USA.
Tel. +1-518-276-6839
E-mail: zhangf2@rpi.edu

Received date: February 04, 2017; Accepted date: March 27, 2017; Published date: April 03, 2017

Citation: Yu Y, Zang N, Zhang F, Linhardt RJ, Zhang H (2017) Proteome Analysis on Proteins Sequentially Extracted from Loach (Misgurnus anguillicaudatus). Biochem Physiol 6: 214. doi: 10.4172/2168-9652.1000214

Copyright: © 2017 Yu Y, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited

Loach (Misgurnus anguillicaudatus) is known as a selenium-rich aquatic product. In present study, a sequential extraction method was applied for separation of water, salt and alkali-soluble proteins from loach (Misgurnus anguillicaudatus). The extracted proteins (included 12 water-soluble, 4 salt-soluble and 7 alkali-soluble proteins) were subjected to molecular weight analysis by SDS-PAGE and MALDI-TOF MS. Then, water soluble proteins were chosen for further ion exchange purification after selenium tracking by ICP-MS. The selenium containing peptides in water soluble proteins were identified by ESI-MS. Four proteins including creatine kinase, cytochrome P450 aromatase, beta-actin and glyceraldehyde 3-phosphate dehydrogenase were identified. Among these proteins, two selenium-containing peptides from beta-actin and cytochrome P450 aromatase were identified. The results of proteome analysis provide valuable molecular information of loach proteins. Moreover, it helps to understand the effect of selenium on redox systems in loach and its antioxidant functions.

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