Trypsin and trypsinogen from an Antarctic fish: molecular basis of cold adaptation.

@article{Genicot1996TrypsinAT,
  title={Trypsin and trypsinogen from an Antarctic fish: molecular basis of cold adaptation.},
  author={Sabine M. Genicot and Françoise Rentier-Delrue and Dianne Edwards and J VanBeeumen and Charles Gerday},
  journal={Biochimica et biophysica acta},
  year={1996},
  volume={1298 1},
  pages={45-57}
}
Trypsin from Antarctic fish Paranotothenia magellanica displays molecular and kinetic properties typical of enzymes produced by psychrophilic organisms. The enzyme has a high catalytic efficiency at low and moderate temperatures and is rapidly inactivated at temperatures higher than 30 degrees C. The nucleotide sequence was determined after mRNA extraction and cDNA synthesis. The cDNA encodes a pretrypsinogen which includes a seven residue activation peptide containing only three acidic… CONTINUE READING