Protein chemical and kinetic characterization of recombinant porcine ribonuclease inhibitor expressed in Saccharomyces cerevisiae.

@article{Vicentini1990ProteinCA,
  title={Protein chemical and kinetic characterization of recombinant porcine ribonuclease inhibitor expressed in Saccharomyces cerevisiae.},
  author={A M Vicentini and Bruno Kieffer and Robert W Matthies and Bernd Meyhack and Brian A. Hemmings and Stuart R. Stone and Jan Hofsteenge},
  journal={Biochemistry},
  year={1990},
  volume={29 37},
  pages={8827-34}
}
A cDNA encoding porcine ribonuclease inhibitor was used to express this protein in yeast under control of the PHO5 promoter. The recombinant protein was purified to homogeneity with a yield of 0.2 mg/g of yeast cells (wet weight) and was found to be indistinguishable from the inhibitor isolated from porcine liver on the basis of the following criteria: the amino acid composition, the number of free sulfhydryl groups, the molecular weight of the native and the denatured protein, peptide mapping… CONTINUE READING

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