Isolation and characterization of two cDNAs from Atlantic cod encoding two distinct psychrophilic elastases

Comp Biochem Physiol B Biochem Mol Biol. 1996 Apr;113(4):795-801. doi: 10.1016/0305-0491(95)02109-4.


The cDNAs encoding two different Atlantic cod elastases have been isolated and sequenced. The predicted amino acid sequences revealed two preproelastases, consisting of a signal peptide, an activation peptide and a mature enzyme of 242 and 239 amino acids. Amino acid sequence identity between the two cod elastases was 60.1% and identity with mammalian elastases ranged from 50-64%. The two cod elastases contain all the major structural features common to serine proteases, such as the catalytic triad His57, Asp102 and Ser195. Both cod elastases have a high content of methionine, consistent with previous findings in psychrophilic fish enzymes.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptation, Physiological*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • Cold Temperature
  • DNA, Complementary / genetics
  • DNA, Complementary / isolation & purification*
  • Fishes / genetics*
  • Fishes / metabolism
  • Humans
  • Isoenzymes / genetics*
  • Molecular Sequence Data
  • Pancreatic Elastase / genetics*
  • Protein Sorting Signals / genetics
  • Sequence Homology, Amino Acid
  • Species Specificity


  • DNA, Complementary
  • Isoenzymes
  • Protein Sorting Signals
  • Pancreatic Elastase