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. Author manuscript; available in PMC: 2013 Jul 15.
Published in final edited form as: Arch Biochem Biophys. 2012 Apr 26;523(2):191–197. doi: 10.1016/j.abb.2012.04.016

Fig. 1.

Fig. 1

Organization of the human SOD2 pre-mRNA and comparison of hMnSOD isoforms A and B. (A) Predicted exon/intron organization of the human SOD2 pre-mRNA. Exon 3 is retained in the variant 1 splicing product, encoding hMnSOD isoform A, but is eliminated from the variant 3 splicing product, encoding hMnSOD isoform B. (B) Alignment of mature protein sequences for hMnSOD isoforms A (bottom) and B (top). Residues that serve as metal ligands in hMnSOD isoform A are indicated by an asterisk (*). (C) Comparison of hMnSOD isoform A (top) and B (bottom) mature proteins, illustrating the different polypeptide lengths.