Purification and some properties of Fe protein of nitrogenase from

Du Daixian; Lin Huimin; He Zhenrong; Dai Lingfen; Xin Wusheng; Li Shanghao

doi:10.1007/BF02849684

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Purification and some properties of Fe protein of nitrogenase from

Updated：2023-05-16

- Purification and some properties of Fe protein of nitrogenase from
- Journal of Oceanology and Limnology Vol. 8, Issue 4, Pages: 378-384(1990)
- Affiliations：
  
  Institute of Hydrobiology
- Author bio：
- Funds：
- DOI：10.1007/BF02849684
  CLC：
- Published：1990
- Accepted：
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Daixian, D., Huimin, L., Zhenrong, H. et al. Purification and some properties of Fe protein of nitrogenase from., Chin. J. Ocean. Limnol. 8, 378–384 (1990). https://doi.org/10.1007/BF02849684
DOI：

Daixian, D., Huimin, L., Zhenrong, H. et al. Purification and some properties of Fe protein of nitrogenase from., Chin. J. Ocean. Limnol. 8, 378–384 (1990). https://doi.org/10.1007/BF02849684 DOI：

摘要

Abstract

The Fe protein ofAnabaena cylindrica was first separated and purified by chromatography through DEAE-cellulose columns then by gel electrophoresis. The specific activity was up to 142.46 nmol C2H4/mg protein · min. It was homogeneous as shown by 1) a single band in the gel electrophorogram; 2) absence of Mo and tryptophan; 3) content of about 3.4 atoms of Fe per mole protein. The molecular weight of the Fe protein ofA. cylindrica was about 61

000 daltons as estimated by SDS-gel electrophoresis and calculated from the amino acid composition. The residues of aspartate and glutamate were about 2.6 times that of arginine and lysine in the Fe protein. Crossing Fe protein ofA. cylindrica with Mo−Fe protein ofAzotobacter vinelandii gave positive result. The reciprocal crossing also showed activity.

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references

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