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Evidence-Based Complementary and Alternative Medicine
Volume 2011, Article ID 965153, 11 pages
Research Article

Molecular Characterization and Expression of α-Globin and β-Globin Genes in the Euryhaline Flounder (Platichthys flesus)

1Key Laboratory of Exploration and Utilization of Aquatic Genetic Resources, Shanghai Ocean University, Shanghai 201306, China
2Laboratory of Adaptive Biology, College of Fisheries and Life Science, Shanghai Ocean University, 999 Huchenghuan Road, Shanghai 201306, China
3Faculty of Life Sciences, The University of Manchester, Oxford Road, Manchester M13 9PT, UK

Received 14 January 2011; Revised 31 March 2011; Accepted 28 June 2011

Copyright © 2011 Weiqun Lu et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

Supplementary Figure 1: Comparison of the predicted amino acid sequences of (a) the flounder β- globin with corresponding chains from previously known α-globin of yellowtail (Okamoto et al., 2001) and human (Michelson and Orkin, 1980) , and (b) the flounder β-globin with β-globin of yellowtail (Okamoto et al., 2001) and human (Lawn et al., 1980). The beginnings and ends of the helical regions, as established for mammalian globins, are indicated by (+) and (-), respectively. The positions of functional residues are indicated by: H, heme binding; 1, α1β1 interfaces; 2, α1β2 interfaces; and B, Bohr effect residues.

Supplementary Figure 2: Negative control for figure 5 & 6. (a) In situ hybridization. The same group of cells showed no specific signal when the specific antisence probe for α-globin and β-globin was replaced with sence probe. (b) Immunocytochemistry. The same group of cells showed no immunoreactivity when the specific primary antiserum for α-globin and β-globin was replaced with preimmune rabbit serum. PT, Proximal tubule.

  1. Supplementary Figures