An aspartic proteinase present in seeds cleaves Arabidopsis 2 S albumin precursors in vitro.

@article{Dhondt1993AnAP,
  title={An aspartic proteinase present in seeds cleaves Arabidopsis 2 S albumin precursors in vitro.},
  author={Kathleen D'hondt and Dustin Bosch and Jozef Van Damme and Mark A. Goethals and Jo{\"e}l Vandekerckhove and Enno Krebbers},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 28},
  pages={20884-91}
}
The Arabidopsis thaliana 2 S albumins are examples of vacuolar proteins which undergo intensive posttranslational processing. An in vitro processing assay to screen for processing enzymes present in seeds was developed using an in vitro synthesized 2 S albumin precursor as the substrate. A protease was characterized which cleaved the substrate into two fragments with molecular weights (as determined from their migration distance on SDS-polyacrylamide gel) corresponding to those of the small and… CONTINUE READING

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