Purification and characterization of a thermostable carboxypeptidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus.

@article{Colombo1992PurificationAC,
  title={Purification and characterization of a thermostable carboxypeptidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus.},
  author={Silvia Colombo and Sabato d'Auria and Paola Alessandra Fusi and Luigi Zecca and Carlo Antonio Raia and Paolo Tortora},
  journal={European journal of biochemistry},
  year={1992},
  volume={206 2},
  pages={
          349-57
        }
}
A carboxypeptidase was purified to electrophoretic homogeneity from the thermoacidophilic archaebacterium Sulfolobus solfataricus. Molecular masses assessed by SDS/PAGE and gel filtration were 42 kDa and 170 kDa, respectively, which points to a tetrameric structure for the molecule. An isoelectric point of 5.9 was also determined. The enzyme was proven to be a metalloprotease, as shown by the inhibitory effects exerted by EDTA and o-phenanthroline; furthermore, dialysis against EDTA led to a… CONTINUE READING

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