@article{oai:nagasaki-u.repo.nii.ac.jp:00014882,
 author = {Wang, Yajun and Osatomi, Kiyoshi and Nagatomo, Yoshimi and Yoshida, Asami and Hara, Kenji},
 issue = {4},
 journal = {Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
 month = {Apr},
 note = {Manganese-superoxide dismutase (Mn-SOD) from Japanese flounder (Paralichthys olivaceus) hepatopancreas has been purified with high purification (781-fold) and recovery (10.8%). The molecular mass of the purified enzyme was estimated to be 26kDa by SDS-PAGE under reducing conditions. In activity staining by native-PAGE, the Japanese flounder Mn-SOD gave three active bands and exhibited KCN-insensitive activity. In addition, the electrophoretic mobility of this enzyme was observed to be faster than that of Japanese flounder Cu,Zn-SOD. On the other hand, the N-terminal amino acid sequence of this Mn-SOD was determined to be 16 amino acid residues, and the sequence showed high homology to other Mn-SODs but not Japanese flounder Cu,Zn-SOD. Analysis of nucleotide and deduced amino acid sequences revealed that the Mn-SOD cDNA consisted of a 64bp 5'-non-coding region, a 675bp open reading frame encoding 225 amino acids, and a 465bp 3'-non-coding region. The first 27 amino acids containing a mitochondria-targeting signal were highly conserved among other Mn-SODs., Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 158(4), pp.289-296; 2011},
 pages = {289--296},
 title = {Purification, molecular cloning, and some properties of a manganese-containing superoxide dismutase from Japanese flounder (Paralichthys olivaceus).},
 volume = {158},
 year = {2011}
}