Human liver manganese superoxide dismutase. Purification and crystallization, subunit association and sulfhydryl reactivity.

@article{Matsuda1990HumanLM,
  title={Human liver manganese superoxide dismutase. Purification and crystallization, subunit association and sulfhydryl reactivity.},
  author={Yoshiro Matsuda and Shinji Higashiyama and Yuko Kijima and Kazuo Suzuki and Keiichi Kawano and Masahiko Akiyama and Sumio Kawata and Seiichiro Tarui and Harold F. Deutsch and Naoyuki Taniguchi},
  journal={European journal of biochemistry},
  year={1990},
  volume={194 3},
  pages={713-20}
}
Manganese superoxide dismutase (Mn-SOD) has been purified with a high yield (320 mg) from human liver (2 kg) and crystallized. Low-angle laser light scattering of the enzyme has shown that native enzyme is a tetrametic form. Four of the eight cysteine residues in the tetramer reacted with 5,5'-dithiobis(2-nitrobenzoic acid) or with iodoacetamide. The others were only reactive in protein heated with SDS or urea after reduction with dithiothreitol or 2-mercaptoethanol. The reactive sulfhydryl… CONTINUE READING