Kiwi protein inhibitor of pectin methylesterase amino-acid sequence and structural importance of two disulfide bridges.

@article{Camardella2000KiwiPI,
  title={Kiwi protein inhibitor of pectin methylesterase amino-acid sequence and structural importance of two disulfide bridges.},
  author={Laura Camardella and Vito Carratore and Maria Antonietta Ciardiello and Luigi Servillo and Ciro Balestrieri and Alfonso Giovane},
  journal={European journal of biochemistry},
  year={2000},
  volume={267 14},
  pages={4561-5}
}
A protein acting as a powerful inhibitor of plant pectin methylesterase was isolated from kiwi (Actinidia chinensis) fruit. The complete amino-acid sequence of the pectin methylesterase inhibitor (PMEI) was determined by direct protein analysis. The sequence comprises 152 amino-acid residues, accounting for a molecular mass of 16 277 Da. The far-UV CD… CONTINUE READING