Aspartic proteinase from barley grains is related to mammalian lysosomal cathepsin D

@article{Sarkkinen1992AsparticPF,
  title={Aspartic proteinase from barley grains is related to mammalian lysosomal cathepsin D},
  author={Paula Sarkkinen and Nisse Kalkkinen and Carola Tilgmann and Jari Siuro and Jukka Kervinen and Leena Mikola},
  journal={Planta},
  year={1992},
  volume={186},
  pages={317-323}
}
Resting barley (Hordeum vulgare L.) grains contain acid-proteinase activity. The corresponding enzyme was purified from grain extracts by affinity chromatography on a pepstatin-Sepharose column. The pH optimum of the affinity-purified enzyme was between 3.5 and 3.9 as measured by hemoglobin hydrolysis and the enzymatic activity was completely inhibited by pepstatin a specific inhibitor of aspartic proteinases (EC 3.4.23). Further purification on a Mono S column followed by activity measurements… CONTINUE READING