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Kiriake, A. and Shiomi, K. (2011). Some properties and cDNA cloning of proteinaceous toxins from two species of lionfish (Pterois antennata and Pterois lunulata). Toxicon, 58: 494-501.

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Article

Proteomic Identification of Stonefish Synanceja verrucosa Venom

1Department of Food Science and Center of Excellence for the Oceans, National Taiwan Ocean University, Keelung, Taiwan, ROC

2Department of Food Science, Yuanpei University, Hsinchu, Taiwan, ROC

3Institute of Biological Chemistry and Genomic Research Center, Academia Sinica, Taipei, Taiwan, ROC

4Department of Health and Nutrition, Asia University, Taichung, Taiwan, ROC


Journal of Food and Nutrition Research. 2015, Vol. 3 No. 8, 526-539
DOI: 10.12691/jfnr-3-8-8
Copyright © 2015 Science and Education Publishing

Cite this paper:
Tai-Yuan Chen, Yu-Huai Chang, Hsi-Pin Lin, Shui-Tein Chen, Deng-Fwu Hwang. Proteomic Identification of Stonefish Synanceja verrucosa Venom. Journal of Food and Nutrition Research. 2015; 3(8):526-539. doi: 10.12691/jfnr-3-8-8.

Correspondence to: Deng-Fwu  Hwang, Department of Food Science and Center of Excellence for the Oceans, National Taiwan Ocean University, Keelung, Taiwan, ROC. Email: dfhwang@mail.ntou.edu.tw

Abstract

Three venom toxins, neoverrucotoxin (neoVTX) α-subunit and β-subunit as well as verrucotoxin (VTX) β-subunit, were identified in the stonefish Synanceja verrucosa by SDS-PAGE, Native-PAGE and two-dimensional electrophoresis (2-DE) coupled with Matrix Assisted Laser Desorption Ionization-Quadrupole-Time-of-Flight (MALDI-Q-TOF). The venom estimated by Native-PAGE were 471, 358, 260 and 166 kDa. The predominate protein bands of crude venom were 84 and 75 kDa by SDS-PAGE. The crude venom protein fell in the region with pI values of 7-9 and molecular weights of 75-90 kDa by 2-DE. Peptide mass fingerprints (PMF) and MS/MS ions originated from MALDI-Q-TOF were used to identify the protein. Our results showed that the complete components of neoverrucotoxin (neoVTX) α-subunit and β-subunit as well as verrucotoxin (VTX) β-subunit were identified from SDS-PAGE and 2-DE patterns. Native-PAGE did not yield protein identifications but revealed the presence of protein complexes.

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