Aspartyl proteases in Caenorhabditis elegans. Isolation, identification and characterization by a combined use of affinity chromatography, two-dimensional gel electrophoresis, microsequencing and databank analysis.

@article{Geier1999AspartylPI,
  title={Aspartyl proteases in Caenorhabditis elegans. Isolation, identification and characterization by a combined use of affinity chromatography, two-dimensional gel electrophoresis, microsequencing and databank analysis.},
  author={Gunter Geier and H. J. Banaj and Hans L. Heid and Luca Bini and Vitaliano Pallini and Robert Zwilling},
  journal={European journal of biochemistry},
  year={1999},
  volume={264 3},
  pages={
          872-9
        }
}
Crude homogenates of the nematode Caenorhabditis elegans exhibit maximal proteolytic activity under acidic pH conditions. About 90% of this activity is inhibited by the oligopeptide pepstatin, which specifically inhibits the activity of aspartyl proteases such as pepsin, cathepsins D and E or renin. We have purified enzymes responsible for this proteolytic activity by a single-step affinity chromatography on pepstatin-agarose. Analysis of the purified fraction by 1D SDS gel electrophoresis… CONTINUE READING
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