Purification and characterization of iron-cofactored superoxide dismutase from Enteromorpha linza

Mingsheng Lü; Ruanhong Cai; Shujun Wang; Zhaopu Liu; Yuliang Jiao; Yaowei Fang; Xiaoxin Zhang

doi:10.1007/s00343-013-3049-3

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Purification and characterization of iron-cofactored superoxide dismutase from Enteromorpha linza

Updated：2023-05-16

- Purification and characterization of iron-cofactored superoxide dismutase from Enteromorpha linza
- Journal of Oceanology and Limnology Vol. 31, Issue 6, Pages: 1190-1195(2013)
- Affiliations：
  
  1. Marine School Huaihai Institute of Technology
  2. College of Resources and Environmental Science Nanjing Agricultural University
- Author bio：
- Funds：
- DOI：10.1007/s00343-013-3049-3
  CLC：
- Online First：31 August 2013，
  
  Published：2013
- Accepted：
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Lü, M., Cai, R., Wang, S. et al. Purification and characterization of iron-cofactored superoxide dismutase from Enteromorpha linza, ., Chin. J. Ocean. Limnol. 31, 1190–1195 (2013). https://doi.org/10.1007/s00343-013-3049-3
DOI：

Lü, M., Cai, R., Wang, S. et al. Purification and characterization of iron-cofactored superoxide dismutase from Enteromorpha linza, ., Chin. J. Ocean. Limnol. 31, 1190–1195 (2013). https://doi.org/10.1007/s00343-013-3049-3 DOI：

摘要

Abstract

A superoxide dismutase was purified from Enteromorpha linza using a simple and safe procedure

which comprised phosphate buffer extraction

ammonium sulphate precipitation

ion exchange chromatography on Q-sepharose column

and gel filtration chromatography on Superdex 200 10/300GL. The E. linza superoxide dismutase (ElSOD) was purified 103.6-fold

and a yield of 19.1% and a specific activity of 1 750 U/mg protein were obtained. The SDS-PAGE exhibited ElSOD a single band near 23 kDa and the gel filtration study showed ElSOD’s molecular weight is near 46 kDa in nondenatured condition

indicating it’s a homodimeric protein. El SOD is an iron-cofactored superoxide dismutase (Fe-SOD) because it was inhibited by hydrogen peroxide

insensitive to potassium cyanide. The optimal temperature for its maximal enzyme activity was 35°C

and it still had 29.8% relative activity at 0°C

then ElSOD can be classified as a cold-adapted enzyme. ElSOD was stable when temperature was below 40°C or the pH was within the range of 5–10. The first 11 N-terminal amino acids of ElSOD were ALELKAPPYEL

comparison of its N-terminal sequence with other Fe-SOD N-terminal sequences at the same position suggests it is possibly a chloroplastic Fe-SOD.

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references

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