The complete sequence, expression in Escherichia coli, purification and some properties of carbonic anhydrase from Neisseria gonorrhoeae.

@article{Chirica1997TheCS,
  title={The complete sequence, expression in Escherichia coli, purification and some properties of carbonic anhydrase from Neisseria gonorrhoeae.},
  author={Laura C Chirica and B Elleby and Bodil Jonsson and Sven Lindskog},
  journal={European journal of biochemistry},
  year={1997},
  volume={244 3},
  pages={755-60}
}
The complete nucleotide sequence of the carbonic anhydrase gene from Neisseria gonorrhoeae has been determined. The gene encodes a 252-residue polypeptide with a molecular mass of 28085 Da. The gene has been cloned and overexpressed in Escherichia coli, and the enzyme has been purified. A 26-residue signal peptide is cleaved off by the E. coli processing machinery. Thus, the isolated enzyme contains 226 amino acid residues with a molecular mass of 25314 Da. Most of the enzyme seems to be… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 23 extracted citations

Acetazolamide protects steatotic liver grafts against cold ischemia reperfusion injury.

The Journal of pharmacology and experimental therapeutics • 2015
View 2 Excerpts

Similar Papers

Loading similar papers…