Primary and secondary structure of antifreeze peptides from arctic and antartic zoarcid fishes

Joseph D. Schrag, Chi Hing C. Cheng, Maria Panico, Howard R. Morris, Arthur L. Deries

Research output: Contribution to journalArticle


Antifreeze peptides were isolated from Rhigophial dearborni, an antartic eel pout, and Lycodes polaris, an arctic eel pout (both from the family Zoarcidae). The primary structures of two peptides, one from each species, were determined using a combination of Edman degradation and mass spectrometric techniques. The two sequences show a high degree of homology with nearly 80% of the residues being identical. These peptides are also homologous to antifreeze peptides from a third eel pout which inhabits the north Atlantic Ocean. The CD spectra of all of these peptides are also very similir. Unlike the antifreeze peptides of cottid fishes, the structures of antifreeze peptides from zoarcid fishes appear to be highly conserved, despite the large geographic distances which separate the different species. The zoarcid peptides also appear to have structures very different from other fish antifreezes.

Original languageEnglish (US)
Pages (from-to)357-370
Number of pages14
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Issue number3
StatePublished - Oct 15 1987


  • (Zoarcid fish)
  • Amino acid sequence
  • Antifreez peptide
  • Cold water fish
  • Ice crystal formation
  • Peptide structure

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Primary and secondary structure of antifreeze peptides from arctic and antartic zoarcid fishes'. Together they form a unique fingerprint.

  • Cite this